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Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, 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J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor"],"title":"PDB code 3bag, chain A, domain 00","aa_length":141.0,"funfam_number":13155,"superfamily_id":"2.80.10.50","ancestor_nodes":"2 2.80 2.80.10 2.80.10.50 2.80.10.50.4 2.80.10.50.4.1 2.80.10.50.4.1.1 2.80.10.50.4.1.1.15 ","keywords":["extracellular space","branch elongation involved in ureteric bud branching","anatomical structure morphogenesis","regulation of endothelial tube morphogenesis","activation of MAPK activity","protein tyrosine kinase activity","positive regulation of cell division","fibroblast growth factor receptor signaling pathway","positive regulation of MAP kinase activity","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","nucleoplasm","S100 protein binding","positive regulation of transcription from RNA polymerase II promoter","positive regulation of cholesterol biosynthetic process","cytosol","regulation of endothelial cell chemotaxis to fibroblast growth factor","growth factor activity","fibroblast growth 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Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"keywords_verbatim":["extracellular space","branch elongation involved in ureteric bud branching","anatomical structure morphogenesis","regulation of endothelial tube morphogenesis","activation of MAPK activity","protein tyrosine kinase activity","positive regulation of cell division","fibroblast growth factor receptor signaling pathway","positive regulation of MAP kinase activity","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","nucleoplasm","S100 protein binding","positive regulation of transcription from RNA polymerase II promoter","positive regulation of cholesterol biosynthetic process","cytosol","regulation of endothelial cell chemotaxis to fibroblast growth factor","growth factor activity","fibroblast growth factor receptor binding","positive regulation of sprouting angiogenesis","mesonephric epithelium development","activation of protein kinase B activity","positive regulation of cell migration","positive regulation of cell proliferation","multicellular organism development","Fibroblast growth factor 1","protein binding","Homo sapiens","regulation of phosphatidylinositol 3-kinase signaling","positive regulation of intracellular signal transduction","Ras guanyl-nucleotide exchange factor activity","positive regulation of angiogenesis","cellular response to heat","MAPK cascade","positive regulation of endothelial cell migration","heparin binding","phosphatidylinositol-mediated signaling","extracellular region","1-phosphatidylinositol-3-kinase activity","integrin binding","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"related_ids":["2.80.10.50","3bag","3bagA","3bagA00","FGF1","FGF1_HUMAN","GO:0000165","GO:0000187","GO:0004713","GO:0005088","GO:0005104","GO:0005178","GO:0005515","GO:0005576","GO:0005615","GO:0005654","GO:0005829","GO:0007275","GO:0008083","GO:0008201","GO:0008284","GO:0008543","GO:0009653","GO:0010595","GO:0014066","GO:0016303","GO:0030335","GO:0032148","GO:0034605","GO:0043406","GO:0044548","GO:0045542","GO:0045766","GO:0045944","GO:0046934","GO:0048015","GO:0051781","GO:0060681","GO:0072163","GO:1901509","GO:1902533","GO:1903672","GO:2000544","P05230","chain:3bagA","domain:3bagA00","goGO:0000165","goGO:0000187","goGO:0004713","goGO:0005088","goGO:0005104","goGO:0005178","goGO:0005515","goGO:0005576","goGO:0005615","goGO:0005654","goGO:0005829","goGO:0007275","goGO:0008083","goGO:0008201","goGO:0008284","goGO:0008543","goGO:0009653","goGO:0010595","goGO:0014066","goGO:0016303","goGO:0030335","goGO:0032148","goGO:0034605","goGO:0043406","goGO:0044548","goGO:0045542","goGO:0045766","goGO:0045944","goGO:0046934","goGO:0048015","goGO:0051781","goGO:0060681","goGO:0072163","goGO:1901509","goGO:1902533","goGO:1903672","goGO:2000544","pdb:3bag","superfamily:2.80.10.50","uniprot:P05230","uniprot_gene_id:FGF1_HUMAN","uniprot_gene_name:FGF1","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230"],"_version_":1591884436182401024},{"funfam_name":"Fibroblast growth factor 2","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3bagB00","content":["3bagB00","PDB code 3bag, chain B, domain 00","regulation of phosphatidylinositol 3-kinase signaling","nucleoplasm","fibroblast growth factor receptor binding","positive regulation of intracellular signal transduction","fibroblast growth factor receptor signaling pathway","activation of protein kinase B activity","MAPK cascade","positive regulation of cell division","cellular response to heat","protein binding","cytosol","extracellular region","positive regulation of cell migration","positive regulation of MAP kinase activity","positive regulation of transcription from RNA polymerase II promoter","extracellular space","1-phosphatidylinositol-3-kinase activity","growth factor activity","anatomical structure morphogenesis","activation of MAPK activity","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","heparin binding","integrin binding","positive regulation of cell proliferation","positive regulation of sprouting angiogenesis","branch elongation involved in ureteric bud branching","phosphatidylinositol-mediated signaling","protein tyrosine kinase activity","Fibroblast growth factor 1","positive regulation of endothelial cell migration","multicellular organism development","regulation of endothelial cell chemotaxis to fibroblast growth factor","mesonephric epithelium development","Homo sapiens","S100 protein binding","Ras guanyl-nucleotide exchange factor activity","positive regulation of angiogenesis","positive regulation of cholesterol biosynthetic process","regulation of endothelial tube morphogenesis","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","2.80.10.50","3bag","3bagB","3bagB00","FGF1","FGF1_HUMAN","GO:0000165","GO:0000187","GO:0004713","GO:0005088","GO:0005104","GO:0005178","GO:0005515","GO:0005576","GO:0005615","GO:0005654","GO:0005829","GO:0007275","GO:0008083","GO:0008201","GO:0008284","GO:0008543","GO:0009653","GO:0010595","GO:0014066","GO:0016303","GO:0030335","GO:0032148","GO:0034605","GO:0043406","GO:0044548","GO:0045542","GO:0045766","GO:0045944","GO:0046934","GO:0048015","GO:0051781","GO:0060681","GO:0072163","GO:1901509","GO:1902533","GO:1903672","GO:2000544","P05230","chain:3bagB","domain:3bagB00","goGO:0000165","goGO:0000187","goGO:0004713","goGO:0005088","goGO:0005104","goGO:0005178","goGO:0005515","goGO:0005576","goGO:0005615","goGO:0005654","goGO:0005829","goGO:0007275","goGO:0008083","goGO:0008201","goGO:0008284","goGO:0008543","goGO:0009653","goGO:0010595","goGO:0014066","goGO:0016303","goGO:0030335","goGO:0032148","goGO:0034605","goGO:0043406","goGO:0044548","goGO:0045542","goGO:0045766","goGO:0045944","goGO:0046934","goGO:0048015","goGO:0051781","goGO:0060681","goGO:0072163","goGO:1901509","goGO:1902533","goGO:1903672","goGO:2000544","pdb:3bag","superfamily:2.80.10.50","uniprot:P05230","uniprot_gene_id:FGF1_HUMAN","uniprot_gene_name:FGF1","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor"],"title":"PDB code 3bag, chain B, domain 00","aa_length":141.0,"funfam_number":13155,"superfamily_id":"2.80.10.50","ancestor_nodes":"2 2.80 2.80.10 2.80.10.50 2.80.10.50.4 2.80.10.50.4.1 2.80.10.50.4.1.1 2.80.10.50.4.1.1.15 ","keywords":["regulation of phosphatidylinositol 3-kinase signaling","nucleoplasm","fibroblast growth factor receptor binding","positive regulation of intracellular signal transduction","fibroblast growth factor receptor signaling pathway","activation of protein kinase B activity","MAPK cascade","positive regulation of cell division","cellular response to heat","protein binding","cytosol","extracellular region","positive regulation of cell migration","positive regulation of MAP kinase activity","positive regulation of transcription from RNA polymerase II promoter","extracellular space","1-phosphatidylinositol-3-kinase activity","growth factor activity","anatomical structure morphogenesis","activation of MAPK activity","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","heparin binding","integrin binding","positive regulation of cell proliferation","positive regulation of sprouting angiogenesis","branch elongation involved in ureteric bud branching","phosphatidylinositol-mediated signaling","protein tyrosine kinase activity","Fibroblast growth factor 1","positive regulation of endothelial cell migration","multicellular organism development","regulation of endothelial cell chemotaxis to fibroblast growth factor","mesonephric epithelium development","Homo sapiens","S100 protein binding","Ras guanyl-nucleotide exchange factor activity","positive regulation of angiogenesis","positive regulation of cholesterol biosynthetic process","regulation of endothelial tube morphogenesis","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"keywords_verbatim":["regulation of phosphatidylinositol 3-kinase signaling","nucleoplasm","fibroblast growth factor receptor binding","positive regulation of intracellular signal transduction","fibroblast growth factor receptor signaling pathway","activation of protein kinase B activity","MAPK cascade","positive regulation of cell division","cellular response to heat","protein binding","cytosol","extracellular region","positive regulation of cell migration","positive regulation of MAP kinase activity","positive regulation of transcription from RNA polymerase II promoter","extracellular space","1-phosphatidylinositol-3-kinase activity","growth factor activity","anatomical structure morphogenesis","activation of MAPK activity","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","heparin binding","integrin binding","positive regulation of cell proliferation","positive regulation of sprouting angiogenesis","branch elongation involved in ureteric bud branching","phosphatidylinositol-mediated signaling","protein tyrosine kinase activity","Fibroblast growth factor 1","positive regulation of endothelial cell migration","multicellular organism development","regulation of endothelial cell chemotaxis to fibroblast growth factor","mesonephric epithelium development","Homo sapiens","S100 protein binding","Ras guanyl-nucleotide exchange factor activity","positive regulation of angiogenesis","positive regulation of cholesterol biosynthetic process","regulation of endothelial tube morphogenesis","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"related_ids":["2.80.10.50","3bag","3bagB","3bagB00","FGF1","FGF1_HUMAN","GO:0000165","GO:0000187","GO:0004713","GO:0005088","GO:0005104","GO:0005178","GO:0005515","GO:0005576","GO:0005615","GO:0005654","GO:0005829","GO:0007275","GO:0008083","GO:0008201","GO:0008284","GO:0008543","GO:0009653","GO:0010595","GO:0014066","GO:0016303","GO:0030335","GO:0032148","GO:0034605","GO:0043406","GO:0044548","GO:0045542","GO:0045766","GO:0045944","GO:0046934","GO:0048015","GO:0051781","GO:0060681","GO:0072163","GO:1901509","GO:1902533","GO:1903672","GO:2000544","P05230","chain:3bagB","domain:3bagB00","goGO:0000165","goGO:0000187","goGO:0004713","goGO:0005088","goGO:0005104","goGO:0005178","goGO:0005515","goGO:0005576","goGO:0005615","goGO:0005654","goGO:0005829","goGO:0007275","goGO:0008083","goGO:0008201","goGO:0008284","goGO:0008543","goGO:0009653","goGO:0010595","goGO:0014066","goGO:0016303","goGO:0030335","goGO:0032148","goGO:0034605","goGO:0043406","goGO:0044548","goGO:0045542","goGO:0045766","goGO:0045944","goGO:0046934","goGO:0048015","goGO:0051781","goGO:0060681","goGO:0072163","goGO:1901509","goGO:1902533","goGO:1903672","goGO:2000544","pdb:3bag","superfamily:2.80.10.50","uniprot:P05230","uniprot_gene_id:FGF1_HUMAN","uniprot_gene_name:FGF1","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAG","RCSB045281","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230"],"_version_":1591884436206518272},{"funfam_name":"Fibroblast growth factor 2","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3bahA00","content":["3bahA00","PDB code 3bah, chain A, domain 00","Fibroblast growth factor 1","anatomical structure morphogenesis","integrin binding","activation of MAPK activity","positive regulation of cholesterol biosynthetic process","regulation of endothelial tube morphogenesis","positive regulation of cell proliferation","extracellular space","positive regulation of sprouting angiogenesis","positive regulation of cell migration","growth factor activity","regulation of phosphatidylinositol 3-kinase signaling","phosphatidylinositol-mediated signaling","positive regulation of intracellular signal transduction","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","MAPK cascade","positive regulation of transcription from RNA polymerase II promoter","cellular response to heat","protein binding","positive regulation of cell division","positive regulation of angiogenesis","mesonephric epithelium development","branch elongation involved in ureteric bud branching","nucleoplasm","S100 protein binding","1-phosphatidylinositol-3-kinase activity","activation of protein kinase B activity","Homo sapiens","extracellular region","protein tyrosine kinase activity","fibroblast growth factor receptor binding","regulation of endothelial cell chemotaxis to fibroblast growth factor","multicellular organism development","cytosol","positive regulation of MAP kinase activity","fibroblast growth factor receptor signaling pathway","Ras guanyl-nucleotide exchange factor activity","positive regulation of endothelial cell migration","heparin binding","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, 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J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor"],"title":"PDB code 3bah, chain A, domain 00","aa_length":141.0,"funfam_number":13155,"superfamily_id":"2.80.10.50","ancestor_nodes":"2 2.80 2.80.10 2.80.10.50 2.80.10.50.4 2.80.10.50.4.1 2.80.10.50.4.1.1 2.80.10.50.4.1.1.11 ","keywords":["Fibroblast growth factor 1","anatomical structure morphogenesis","integrin binding","activation of MAPK activity","positive regulation of cholesterol biosynthetic process","regulation of endothelial tube morphogenesis","positive regulation of cell proliferation","extracellular space","positive regulation of sprouting angiogenesis","positive regulation of cell migration","growth factor activity","regulation of phosphatidylinositol 3-kinase signaling","phosphatidylinositol-mediated signaling","positive regulation of intracellular signal transduction","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","MAPK cascade","positive regulation of transcription from RNA polymerase II promoter","cellular response to heat","protein binding","positive regulation of cell division","positive regulation of angiogenesis","mesonephric epithelium development","branch elongation involved in ureteric bud branching","nucleoplasm","S100 protein binding","1-phosphatidylinositol-3-kinase activity","activation of protein kinase B activity","Homo sapiens","extracellular region","protein tyrosine kinase activity","fibroblast growth factor receptor binding","regulation of endothelial cell chemotaxis to fibroblast growth factor","multicellular organism development","cytosol","positive regulation of MAP kinase activity","fibroblast growth factor receptor signaling pathway","Ras guanyl-nucleotide exchange factor activity","positive regulation of endothelial cell migration","heparin binding","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"keywords_verbatim":["Fibroblast growth factor 1","anatomical structure morphogenesis","integrin binding","activation of MAPK activity","positive regulation of cholesterol biosynthetic process","regulation of endothelial tube morphogenesis","positive regulation of cell proliferation","extracellular space","positive regulation of sprouting angiogenesis","positive regulation of cell migration","growth factor activity","regulation of phosphatidylinositol 3-kinase signaling","phosphatidylinositol-mediated signaling","positive regulation of intracellular signal transduction","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","MAPK cascade","positive regulation of transcription from RNA polymerase II promoter","cellular response to heat","protein binding","positive regulation of cell division","positive regulation of angiogenesis","mesonephric epithelium development","branch elongation involved in ureteric bud branching","nucleoplasm","S100 protein binding","1-phosphatidylinositol-3-kinase activity","activation of protein kinase B activity","Homo sapiens","extracellular region","protein tyrosine kinase activity","fibroblast growth factor receptor binding","regulation of endothelial cell chemotaxis to fibroblast growth factor","multicellular organism development","cytosol","positive regulation of MAP kinase activity","fibroblast growth factor receptor signaling pathway","Ras guanyl-nucleotide exchange factor activity","positive regulation of endothelial cell migration","heparin binding","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"related_ids":["2.80.10.50","3bah","3bahA","3bahA00","FGF1","FGF1_HUMAN","GO:0000165","GO:0000187","GO:0004713","GO:0005088","GO:0005104","GO:0005178","GO:0005515","GO:0005576","GO:0005615","GO:0005654","GO:0005829","GO:0007275","GO:0008083","GO:0008201","GO:0008284","GO:0008543","GO:0009653","GO:0010595","GO:0014066","GO:0016303","GO:0030335","GO:0032148","GO:0034605","GO:0043406","GO:0044548","GO:0045542","GO:0045766","GO:0045944","GO:0046934","GO:0048015","GO:0051781","GO:0060681","GO:0072163","GO:1901509","GO:1902533","GO:1903672","GO:2000544","P05230","chain:3bahA","domain:3bahA00","goGO:0000165","goGO:0000187","goGO:0004713","goGO:0005088","goGO:0005104","goGO:0005178","goGO:0005515","goGO:0005576","goGO:0005615","goGO:0005654","goGO:0005829","goGO:0007275","goGO:0008083","goGO:0008201","goGO:0008284","goGO:0008543","goGO:0009653","goGO:0010595","goGO:0014066","goGO:0016303","goGO:0030335","goGO:0032148","goGO:0034605","goGO:0043406","goGO:0044548","goGO:0045542","goGO:0045766","goGO:0045944","goGO:0046934","goGO:0048015","goGO:0051781","goGO:0060681","goGO:0072163","goGO:1901509","goGO:1902533","goGO:1903672","goGO:2000544","pdb:3bah","superfamily:2.80.10.50","uniprot:P05230","uniprot_gene_id:FGF1_HUMAN","uniprot_gene_name:FGF1","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230"],"_version_":1591884436327104512},{"funfam_name":"Fibroblast growth factor 2","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3bahB00","content":["3bahB00","PDB code 3bah, chain B, domain 00","positive regulation of cell proliferation","phosphatidylinositol-mediated signaling","multicellular organism development","fibroblast growth factor receptor signaling pathway","cytosol","cellular response to heat","positive regulation of intracellular signal transduction","fibroblast growth factor receptor binding","anatomical structure morphogenesis","regulation of endothelial cell chemotaxis to fibroblast growth factor","MAPK cascade","Homo sapiens","regulation of phosphatidylinositol 3-kinase signaling","heparin binding","extracellular space","positive regulation of sprouting angiogenesis","S100 protein binding","positive regulation of MAP kinase activity","mesonephric epithelium development","positive regulation of transcription from RNA polymerase II promoter","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","positive regulation of cell division","branch elongation involved in ureteric bud branching","integrin binding","extracellular region","positive regulation of angiogenesis","1-phosphatidylinositol-3-kinase activity","Fibroblast growth factor 1","growth factor activity","activation of protein kinase B activity","Ras guanyl-nucleotide exchange factor activity","protein binding","nucleoplasm","positive regulation of endothelial cell migration","regulation of endothelial tube morphogenesis","positive regulation of cell migration","activation of MAPK activity","protein tyrosine kinase activity","positive regulation of cholesterol biosynthetic process","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","2.80.10.50","3bah","3bahB","3bahB00","FGF1","FGF1_HUMAN","GO:0000165","GO:0000187","GO:0004713","GO:0005088","GO:0005104","GO:0005178","GO:0005515","GO:0005576","GO:0005615","GO:0005654","GO:0005829","GO:0007275","GO:0008083","GO:0008201","GO:0008284","GO:0008543","GO:0009653","GO:0010595","GO:0014066","GO:0016303","GO:0030335","GO:0032148","GO:0034605","GO:0043406","GO:0044548","GO:0045542","GO:0045766","GO:0045944","GO:0046934","GO:0048015","GO:0051781","GO:0060681","GO:0072163","GO:1901509","GO:1902533","GO:1903672","GO:2000544","P05230","chain:3bahB","domain:3bahB00","goGO:0000165","goGO:0000187","goGO:0004713","goGO:0005088","goGO:0005104","goGO:0005178","goGO:0005515","goGO:0005576","goGO:0005615","goGO:0005654","goGO:0005829","goGO:0007275","goGO:0008083","goGO:0008201","goGO:0008284","goGO:0008543","goGO:0009653","goGO:0010595","goGO:0014066","goGO:0016303","goGO:0030335","goGO:0032148","goGO:0034605","goGO:0043406","goGO:0044548","goGO:0045542","goGO:0045766","goGO:0045944","goGO:0046934","goGO:0048015","goGO:0051781","goGO:0060681","goGO:0072163","goGO:1901509","goGO:1902533","goGO:1903672","goGO:2000544","pdb:3bah","superfamily:2.80.10.50","uniprot:P05230","uniprot_gene_id:FGF1_HUMAN","uniprot_gene_name:FGF1","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor","Lee, J.","Blaber, M.","J.Mol.Biol.","A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.","2008","Lee, J.","Dubey, V.K.","Longo, L.M.","Blaber, M.","Heparin-binding growth factor 1","Crystal structure of K112N mutant of Human acidic fibroblast growth factor"],"title":"PDB code 3bah, chain B, domain 00","aa_length":142.0,"funfam_number":13155,"superfamily_id":"2.80.10.50","ancestor_nodes":"2 2.80 2.80.10 2.80.10.50 2.80.10.50.4 2.80.10.50.4.1 2.80.10.50.4.1.1 2.80.10.50.4.1.1.11 ","keywords":["positive regulation of cell proliferation","phosphatidylinositol-mediated signaling","multicellular organism development","fibroblast growth factor receptor signaling pathway","cytosol","cellular response to heat","positive regulation of intracellular signal transduction","fibroblast growth factor receptor binding","anatomical structure morphogenesis","regulation of endothelial cell chemotaxis to fibroblast growth factor","MAPK cascade","Homo sapiens","regulation of phosphatidylinositol 3-kinase signaling","heparin binding","extracellular space","positive regulation of sprouting angiogenesis","S100 protein binding","positive regulation of MAP kinase activity","mesonephric epithelium development","positive regulation of transcription from RNA polymerase II promoter","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","positive regulation of cell division","branch elongation involved in ureteric bud branching","integrin binding","extracellular region","positive regulation of angiogenesis","1-phosphatidylinositol-3-kinase activity","Fibroblast growth factor 1","growth factor activity","activation of protein kinase B activity","Ras guanyl-nucleotide exchange factor activity","protein binding","nucleoplasm","positive regulation of endothelial cell migration","regulation of endothelial tube morphogenesis","positive regulation of cell migration","activation of MAPK activity","protein tyrosine kinase activity","positive regulation of cholesterol biosynthetic process","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"keywords_verbatim":["positive regulation of cell proliferation","phosphatidylinositol-mediated signaling","multicellular organism development","fibroblast growth factor receptor signaling pathway","cytosol","cellular response to heat","positive regulation of intracellular signal transduction","fibroblast growth factor receptor binding","anatomical structure morphogenesis","regulation of endothelial cell chemotaxis to fibroblast growth factor","MAPK cascade","Homo sapiens","regulation of phosphatidylinositol 3-kinase signaling","heparin binding","extracellular space","positive regulation of sprouting angiogenesis","S100 protein binding","positive regulation of MAP kinase activity","mesonephric epithelium development","positive regulation of transcription from RNA polymerase II promoter","phosphatidylinositol-4,5-bisphosphate 3-kinase activity","positive regulation of cell division","branch elongation involved in ureteric bud branching","integrin binding","extracellular region","positive regulation of angiogenesis","1-phosphatidylinositol-3-kinase activity","Fibroblast growth factor 1","growth factor activity","activation of protein kinase B activity","Ras guanyl-nucleotide exchange factor activity","protein binding","nucleoplasm","positive regulation of endothelial cell migration","regulation of endothelial tube morphogenesis","positive regulation of cell migration","activation of MAPK activity","protein tyrosine kinase activity","positive regulation of cholesterol biosynthetic process","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE","Heparin-binding growth factor 1","polymer","FORMIC ACID","non-polymer","water","water","polypeptide(L)","human","Homo","FGF1, FGFA","Homo sapiens","monomeric","monomeric","HORMONE","beta-trefoil, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, HORMONE"],"related_ids":["2.80.10.50","3bah","3bahB","3bahB00","FGF1","FGF1_HUMAN","GO:0000165","GO:0000187","GO:0004713","GO:0005088","GO:0005104","GO:0005178","GO:0005515","GO:0005576","GO:0005615","GO:0005654","GO:0005829","GO:0007275","GO:0008083","GO:0008201","GO:0008284","GO:0008543","GO:0009653","GO:0010595","GO:0014066","GO:0016303","GO:0030335","GO:0032148","GO:0034605","GO:0043406","GO:0044548","GO:0045542","GO:0045766","GO:0045944","GO:0046934","GO:0048015","GO:0051781","GO:0060681","GO:0072163","GO:1901509","GO:1902533","GO:1903672","GO:2000544","P05230","chain:3bahB","domain:3bahB00","goGO:0000165","goGO:0000187","goGO:0004713","goGO:0005088","goGO:0005104","goGO:0005178","goGO:0005515","goGO:0005576","goGO:0005615","goGO:0005654","goGO:0005829","goGO:0007275","goGO:0008083","goGO:0008201","goGO:0008284","goGO:0008543","goGO:0009653","goGO:0010595","goGO:0014066","goGO:0016303","goGO:0030335","goGO:0032148","goGO:0034605","goGO:0043406","goGO:0044548","goGO:0045542","goGO:0045766","goGO:0045944","goGO:0046934","goGO:0048015","goGO:0051781","goGO:0060681","goGO:0072163","goGO:1901509","goGO:1902533","goGO:1903672","goGO:2000544","pdb:3bah","superfamily:2.80.10.50","uniprot:P05230","uniprot_gene_id:FGF1_HUMAN","uniprot_gene_name:FGF1","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","10.1016/j.jmb.2008.01.055","18308335","3BAH","RCSB045282","9606","FGF1_HUMAN","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230","P05230"],"_version_":1591884436352270336},{"funfam_name":"Alpha-amylase 1","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3baiA01","content":["3baiA01","PDB code 3bai, chain A, domain 01","chloride ion binding","extracellular space","Pancreatic alpha-amylase","extracellular region","alpha-amylase activity","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","polysaccharide digestion","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","Glycogenase.","extracellular exosome","Alpha-amylase.","calcium ion binding","carbohydrate catabolic process","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","3.2.1.1","3.20.20.80","3bai","3baiA","3baiA01","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3baiA","domain:3baiA01","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bai","superfamily:3.20.20.80","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate"],"superfamily_name":"Glycosidases","title":"PDB code 3bai, chain A, domain 01","aa_length":402.0,"funfam_number":53135,"superfamily_id":"3.20.20.80","ancestor_nodes":"3 3.20 3.20.20 3.20.20.80 3.20.20.80.27 3.20.20.80.27.1 3.20.20.80.27.1.1 3.20.20.80.27.1.1.16 ","keywords":["chloride ion binding","extracellular space","Pancreatic alpha-amylase","extracellular region","alpha-amylase activity","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","polysaccharide digestion","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","Glycogenase.","extracellular exosome","Alpha-amylase.","calcium ion binding","carbohydrate catabolic process","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"keywords_verbatim":["chloride ion binding","extracellular space","Pancreatic alpha-amylase","extracellular region","alpha-amylase activity","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","polysaccharide digestion","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","Glycogenase.","extracellular exosome","Alpha-amylase.","calcium ion binding","carbohydrate catabolic process","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"related_ids":["3.2.1.1","3.20.20.80","3bai","3baiA","3baiA01","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3baiA","domain:3baiA01","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bai","superfamily:3.20.20.80","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746"],"_version_":1591884436422524928},{"funfam_name":"Pot. pancreatic alpha-amylase isozyme","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3baiA02","content":["3baiA02","PDB code 3bai, chain A, domain 02","Alpha-amylase.","extracellular region","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","alpha-amylase activity","Pancreatic alpha-amylase","polysaccharide digestion","extracellular exosome","carbohydrate catabolic process","chloride ion binding","extracellular space","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","calcium ion binding","Glycogenase.","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","2.60.40.1180","3.2.1.1","3bai","3baiA","3baiA02","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3baiA","domain:3baiA02","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bai","superfamily:2.60.40.1180","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha Amylase with Bound Nitrate"],"superfamily_name":"Golgi alpha-mannosidase II","title":"PDB code 3bai, chain A, domain 02","aa_length":93.0,"funfam_number":13698,"superfamily_id":"2.60.40.1180","ancestor_nodes":"2 2.60 2.60.40 2.60.40.1180 2.60.40.1180.2 2.60.40.1180.2.1 2.60.40.1180.2.1.1 2.60.40.1180.2.1.1.1 ","keywords":["Alpha-amylase.","extracellular region","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","alpha-amylase activity","Pancreatic alpha-amylase","polysaccharide digestion","extracellular exosome","carbohydrate catabolic process","chloride ion binding","extracellular space","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","calcium ion binding","Glycogenase.","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"keywords_verbatim":["Alpha-amylase.","extracellular region","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","alpha-amylase activity","Pancreatic alpha-amylase","polysaccharide digestion","extracellular exosome","carbohydrate catabolic process","chloride ion binding","extracellular space","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","calcium ion binding","Glycogenase.","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Diabetes, Human, Pancreatic, Enzyme, Anion Activation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Hydrolase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"related_ids":["2.60.40.1180","3.2.1.1","3bai","3baiA","3baiA02","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3baiA","domain:3baiA02","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bai","superfamily:2.60.40.1180","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAI","RCSB045283","9606","AMYP_HUMAN","P04746","P04746","P04746"],"_version_":1591884436443496448},{"funfam_name":"Alpha-amylase 1","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3bajA01","content":["3bajA01","PDB code 3baj, chain A, domain 01","Glycogenase.","polysaccharide digestion","calcium ion binding","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Alpha-amylase.","chloride ion binding","Pancreatic alpha-amylase","extracellular space","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","extracellular region","alpha-amylase activity","extracellular exosome","carbohydrate catabolic process","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","3.2.1.1","3.20.20.80","3baj","3bajA","3bajA01","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bajA","domain:3bajA01","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3baj","superfamily:3.20.20.80","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose"],"superfamily_name":"Glycosidases","title":"PDB code 3baj, chain A, domain 01","aa_length":402.0,"funfam_number":53135,"superfamily_id":"3.20.20.80","ancestor_nodes":"3 3.20 3.20.20 3.20.20.80 3.20.20.80.27 3.20.20.80.27.1 3.20.20.80.27.1.1 3.20.20.80.27.1.1.38 ","keywords":["Glycogenase.","polysaccharide digestion","calcium ion binding","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Alpha-amylase.","chloride ion binding","Pancreatic alpha-amylase","extracellular space","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","extracellular region","alpha-amylase activity","extracellular exosome","carbohydrate catabolic process","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"keywords_verbatim":["Glycogenase.","polysaccharide digestion","calcium ion binding","Homo sapiens","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Alpha-amylase.","chloride ion binding","Pancreatic alpha-amylase","extracellular space","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","extracellular region","alpha-amylase activity","extracellular exosome","carbohydrate catabolic process","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"related_ids":["3.2.1.1","3.20.20.80","3baj","3bajA","3bajA01","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bajA","domain:3bajA01","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3baj","superfamily:3.20.20.80","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746"],"_version_":1591884436502216704},{"funfam_name":"Pot. pancreatic alpha-amylase isozyme","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3bajA02","content":["3bajA02","PDB code 3baj, chain A, domain 02","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","calcium ion binding","Homo sapiens","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","Glycogenase.","Alpha-amylase.","polysaccharide digestion","carbohydrate catabolic process","extracellular exosome","chloride ion binding","Pancreatic alpha-amylase","extracellular space","extracellular region","alpha-amylase activity","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","2.60.40.1180","3.2.1.1","3baj","3bajA","3bajA02","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bajA","domain:3bajA02","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3baj","superfamily:2.60.40.1180","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose"],"superfamily_name":"Golgi alpha-mannosidase II","title":"PDB code 3baj, chain A, domain 02","aa_length":93.0,"funfam_number":13698,"superfamily_id":"2.60.40.1180","ancestor_nodes":"2 2.60 2.60.40 2.60.40.1180 2.60.40.1180.2 2.60.40.1180.2.1 2.60.40.1180.2.1.1 2.60.40.1180.2.1.1.1 ","keywords":["-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","calcium ion binding","Homo sapiens","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","Glycogenase.","Alpha-amylase.","polysaccharide digestion","carbohydrate catabolic process","extracellular exosome","chloride ion binding","Pancreatic alpha-amylase","extracellular space","extracellular region","alpha-amylase activity","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"keywords_verbatim":["-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","calcium ion binding","Homo sapiens","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","Glycogenase.","Alpha-amylase.","polysaccharide digestion","carbohydrate catabolic process","extracellular exosome","chloride ion binding","Pancreatic alpha-amylase","extracellular space","extracellular region","alpha-amylase activity","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","SUGAR (ACARBOSE DERIVED PENTASACCHARIDE)","non-polymer","NITRATE ION","non-polymer","CALCIUM ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Human, Pancreatic, Enzyme, Hydrolase, Acarbose, Transglycosylation, Chloride, Nitrate, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"related_ids":["2.60.40.1180","3.2.1.1","3baj","3bajA","3bajA02","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bajA","domain:3bajA02","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3baj","superfamily:2.60.40.1180","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAJ","RCSB045284","9606","AMYP_HUMAN","P04746","P04746","P04746"],"_version_":1591884436525285376},{"funfam_name":"Alpha-amylase 1","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3bakA01","content":["3bakA01","PDB code 3bak, chain A, domain 01","polysaccharide digestion","chloride ion binding","extracellular space","alpha-amylase activity","Homo sapiens","carbohydrate catabolic process","Glycogenase.","Alpha-amylase.","extracellular region","Pancreatic alpha-amylase","extracellular exosome","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","calcium ion binding","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","3.2.1.1","3.20.20.80","3bak","3bakA","3bakA01","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bakA","domain:3bakA01","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bak","superfamily:3.20.20.80","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate"],"superfamily_name":"Glycosidases","title":"PDB code 3bak, chain A, domain 01","aa_length":402.0,"funfam_number":53135,"superfamily_id":"3.20.20.80","ancestor_nodes":"3 3.20 3.20.20 3.20.20.80 3.20.20.80.27 3.20.20.80.27.1 3.20.20.80.27.1.1 3.20.20.80.27.1.1.17 ","keywords":["polysaccharide digestion","chloride ion binding","extracellular space","alpha-amylase activity","Homo sapiens","carbohydrate catabolic process","Glycogenase.","Alpha-amylase.","extracellular region","Pancreatic alpha-amylase","extracellular exosome","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","calcium ion binding","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"keywords_verbatim":["polysaccharide digestion","chloride ion binding","extracellular space","alpha-amylase activity","Homo sapiens","carbohydrate catabolic process","Glycogenase.","Alpha-amylase.","extracellular region","Pancreatic alpha-amylase","extracellular exosome","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","calcium ion binding","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"related_ids":["3.2.1.1","3.20.20.80","3bak","3bakA","3bakA01","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bakA","domain:3bakA01","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bak","superfamily:3.20.20.80","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746"],"_version_":1591884436587151360},{"funfam_name":"Pot. pancreatic alpha-amylase isozyme","status":"UNKNOWN","doc_type":"domain","date_created":"2013-03-26T12:05:23Z","node_depth":9,"id":"3bakA02","content":["3bakA02","PDB code 3bak, chain A, domain 02","Glycogenase.","chloride ion binding","carbohydrate catabolic process","extracellular exosome","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Pancreatic alpha-amylase","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","polysaccharide digestion","calcium ion binding","alpha-amylase activity","Alpha-amylase.","extracellular space","Homo sapiens","extracellular region","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","2.60.40.1180","3.2.1.1","3bak","3bakA","3bakA02","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bakA","domain:3bakA02","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bak","superfamily:2.60.40.1180","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate","Fredriksen, J.R.","Maurus, R.","Brayer, G.D.","Biochemistry","Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","2008","Maurus, R.","Begum, A.","Williams, L.K.","Fredriksen, J.R.","Zhang, R.","Withers, S.G.","Brayer, G.D.","Pancreatic alpha-amylase (E.C.3.2.1.1)","N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate"],"superfamily_name":"Golgi alpha-mannosidase II","title":"PDB code 3bak, chain A, domain 02","aa_length":93.0,"funfam_number":13698,"superfamily_id":"2.60.40.1180","ancestor_nodes":"2 2.60 2.60.40 2.60.40.1180 2.60.40.1180.2 2.60.40.1180.2.1 2.60.40.1180.2.1.1 2.60.40.1180.2.1.1.1 ","keywords":["Glycogenase.","chloride ion binding","carbohydrate catabolic process","extracellular exosome","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Pancreatic alpha-amylase","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","polysaccharide digestion","calcium ion binding","alpha-amylase activity","Alpha-amylase.","extracellular space","Homo sapiens","extracellular region","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"keywords_verbatim":["Glycogenase.","chloride ion binding","carbohydrate catabolic process","extracellular exosome","-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.","Pancreatic alpha-amylase","Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.","polysaccharide digestion","calcium ion binding","alpha-amylase activity","Alpha-amylase.","extracellular space","Homo sapiens","extracellular region","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted","Pancreatic alpha-amylase","polymer","SUGAR (N-ACETYL-D-GLUCOSAMINE)","non-polymer","CALCIUM ION","non-polymer","NITRATE ION","non-polymer","water","water","polypeptide(L)","human","Homo","AMY2A","Homo sapiens","monomeric","HYDROLASE","Amylase, Anion Activation, Chloride, Nitrate, Hydrolase, Human, Pancreatic, Enzyme, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted"],"related_ids":["2.60.40.1180","3.2.1.1","3bak","3bakA","3bakA02","AMY2A","AMYP_HUMAN","GO:0004556","GO:0005509","GO:0005576","GO:0005615","GO:0016052","GO:0031404","GO:0044245","GO:0070062","P04746","chain:3bakA","domain:3bakA02","ec:3.2.1.1","goGO:0004556","goGO:0005509","goGO:0005576","goGO:0005615","goGO:0016052","goGO:0031404","goGO:0044245","goGO:0070062","pdb:3bak","superfamily:2.60.40.1180","uniprot:P04746","uniprot_gene_id:AMYP_HUMAN","uniprot_gene_name:AMY2A","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746","10.1021/bi701652t","18284212","3BAK","RCSB045285","9606","AMYP_HUMAN","P04746","P04746","P04746","P04746"],"_version_":1591884436608122880}]},"facet_counts":{"facet_queries":{},"facet_fields":{"keywords_verbatim":{"polymer":530015,"polypeptide(L)":530009,"water":439242,"non-polymer":419299,"dimeric":173955,"protein binding":171200,"monomeric":157636,"Homo sapiens":137363,"cytosol":95417,"human":81383,"MAGNESIUM ION":78013,"tetrameric":75537,"SULFATE ION":66336,"HYDROLASE":64075,"ZINC ION":60559,"plasma membrane":57643,"GLYCEROL":57216,"TRANSFERASE":56684,"nucleus":54697,"OXIDOREDUCTASE":52926,"cytoplasm":52808,"extracellular exosome":48450,"CHLORIDE ION":46907,"nucleoplasm":45311,"trimeric":44127,"identical protein binding":43346,"CALCIUM ION":40721,"double helix":39051,"Escherichia coli K-12":35351,"extracellular region":34745,"Homo":34156,"Escherichia coli":32394,"hexameric":31105,"SODIUM ION":28864,"membrane":28320,"extracellular space":28205,"polyribonucleotide":27557,"a-form double helix":26775,"mismatched base pair":26525,"1,2-ETHANEDIOL":25562,"Saccharomyces cerevisiae S288C":22214,"Mus musculus":22159,"hairpin loop":21877,"PHOSPHATE ION":21354,"triple helix":20992,"internal loop":20926,"bulge loop":20736,"protein homodimerization activity":20320,"polydeoxyribonucleotide":20181,"four-way junction":19741,"IMMUNE SYSTEM":19704,"tetraloop":19626,"quadruple helix":19591,"three-way junction":19510,"SUGAR (N-ACETYL-D-GLUCOSAMINE)":19060,"b-form double helix":18870,"HOMO SAPIENS":18436,"HUMAN":17952,"PROTOPORPHYRIN IX CONTAINING FE":17641,"LYASE":17434,"parallel strands":17051,"Escherichia":16973,"Human":16770,"ACETATE ION":16595,"protein complex":16528,"RIBOSOME":15933,"enzyme binding":15882,"mitochondrion":15690,"zinc ion binding":15203,"neutrophil degranulation":14981,"RNA binding":14212,"negative regulation of apoptotic process":13731,"POTASSIUM ION":13553,"ATP + a protein = ADP + a phosphoprotein.":13267,"SUGAR (2-MER)":13225,"positive regulation of transcription from RNA polymerase II promoter":13180,"Uncharacterized protein":13065,"HYDROLASE/HYDROLASE INHIBITOR":13041,"Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).":12930,"Rattus norvegicus":12833,"-!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49.":12643,"DNA nucleotidyltransferase (DNA-directed). DNA-dependent DNA polymerase.":12643,"DNA-directed DNA polymerase.":12643,"integral component of plasma membrane":12550,"signal transduction":12537,"cell surface":12505,"MANGANESE (II) ION":12334,"Bos taurus":12294,"octameric":12255,"magnesium ion binding":11564,"Golgi apparatus":11471,"ATP binding":11470,"proteolysis":11419,"Saccharomyces cerevisiae":11132,"cellular protein metabolic process":11127,"protein serine/threonine kinase activity":11102,"ADENOSINE-5'-DIPHOSPHATE":11028,"protein phosphorylation":10908,"FLAVIN-ADENINE DINUCLEOTIDE":10864,"TRANSPORT PROTEIN":10579,"TRANSCRIPTION":10416,"DNA binding":10357,"proteasome-mediated ubiquitin-dependent protein catabolic process":10338,"positive regulation of cell proliferation":10049,"receptor binding":10031,"ISOMERASE":9992,"cellular response to DNA damage stimulus":9964,"endoplasmic reticulum":9662,"focal adhesion":9430,"endoplasmic reticulum lumen":9403,"serine-type endopeptidase activity":9352,"pentameric":9235,"protein kinase binding":9059,"LIGASE":8955,"DI(HYDROXYETHYL)ETHER":8764,"Mycobacterium tuberculosis H37Rv":8730,"Acting on ester bonds.":8634,"negative regulation of transcription from RNA polymerase II promoter":8597,"perinuclear region of cytoplasm":8568,"positive regulation of transcription, DNA-templated":8514,"dodecameric":8512,"protein deubiquitination":8227,"K12":8212,"blood microparticle":8201,"Thermus thermophilus HB8":8155,"-!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.":8076,"Cleavage of peptide bonds with very broad specificity.":8076,"Ingensin. Lens neutral proteinase. Macropain. Multicatalytic endopeptidase complex. Multicatalytic proteinase (complex). Prosome. Proteasome.":8076,"Proteasome endopeptidase complex.":8076,"-!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70.":7863,"Non-specific serine/threonine protein kinase.":7863,"Protein phosphokinase. Protein serine kinase. Protein serine-threonine kinase. Protein-serine kinase. Serine kinase. Serine protein kinase. Serine(threonine) protein kinase. Serine-specific protein kinase. Serine/threonine protein kinase. Threonine-specific protein kinase.":7863,"SUGAR (3-MER)":7730,"protein heterodimerization activity":7692,"SIGNALING PROTEIN":7676,"protein domain specific binding":7557,"calcium ion binding":7305,"MAPK cascade":7274,"VIRAL PROTEIN":7200,"mouse":7155,"endoplasmic reticulum membrane":7122,"protein autophosphorylation":7086,"protein kinase activity":7085,"ficolin-1-rich granule lumen":7039,"2-(N-MORPHOLINO)-ETHANESULFONIC ACID":7026,"proteasomal ubiquitin-independent protein catabolic process":7013,"NICOTINAMIDE-ADENINE-DINUCLEOTIDE":6952,"house mouse":6833,"ubiquitin protein ligase binding":6740,"Bacillus subtilis subsp. subtilis str. 168":6706,"negative regulation of cell proliferation":6677,"negative regulation of transcription, DNA-templated":6675,"positive regulation of gene expression":6636,"Mycobacterium tuberculosis":6629,"Pseudomonas aeruginosa PAO1":6620,"FE (III) ION":6600,"Mus":6574,"transcription factor binding":6394,"regulation of signal transduction by p53 class mediator":6318,"nucleolus":6314,"ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.":6286,"blood coagulation":6220,"ADENOSINE-5'-TRIPHOSPHATE":6031,"STRUCTURAL GENOMICS, UNKNOWN FUNCTION":5990,"positive regulation of protein phosphorylation":5983,"regulation of immune response":5946,"heme binding":5918,"Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).":5913,"cadherin binding":5913,"protein tyrosine kinase activity":5901,"intracellular membrane-bounded organelle":5897,"post-translational protein modification":5876,"secretory granule lumen":5860,"Nucleotidyltransferases.":5827,"IRON/SULFUR CLUSTER":5826,"COPPER (II) ION":5804,"TRANSFERASE/TRANSFERASE INHIBITOR":5703,"Thermus thermophilus":5664,"centrosome":5608,"MEMBRANE PROTEIN":5599,"cell proliferation":5533,"decameric":5528,"leukocyte migration":5459,"CADMIUM ION":5441,"ATPase activity":5426,"positive regulation of cell migration":5411,"PROTEIN BINDING":5394,"peptidase activity":5375,"-!- Catalyzes RNA-template-directed extension of the 3'-end of a DNA strand by one deoxynucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a RNA or DNA primer. -!- DNA can also serve as template. -!- See also EC 2.7.7.7.":5323,"DNA nucleotidyltransferase (RNA-directed). Reverse transcriptase. Revertase.":5323,"RNA-directed DNA polymerase.":5323,"protein ubiquitination":5315,"chromatin binding":5277,"24-meric":5276,"Gallus gallus":5273,"kinase activity":5270,"cell surface receptor signaling pathway":5267,"(4S)-2-METHYL-2,4-PENTANEDIOL":5238,"DIMETHYL SULFOXIDE":5237,"Golgi membrane":5236,"FE2/S2 (INORGANIC) CLUSTER":5206,"endosome":5179,"innate immune response":5161,"28-meric":5150,"mitochondrial matrix":5141,"Beta-2-microglobulin":5093,"transcription from RNA polymerase II promoter":5075,"Staphylococcus aureus":5074,"30S ribosomal protein S2":5046,"30S ribosomal protein S4":5027,"30S ribosomal protein S5":5026,"30S ribosomal protein S13":5021,"30S ribosomal protein S3":5020,"Pseudomonas aeruginosa":5003,"30S ribosomal protein S10":4986,"Thermotoga maritima MSB8":4981,"Bacillus":4975,"30S ribosomal protein S7":4966,"Fc-epsilon receptor signaling pathway":4966,"30S ribosomal protein S11":4962,"30S ribosomal protein S18":4957,"30S ribosomal protein S6":4956,"30S ribosomal protein S16":4955,"30S ribosomal protein S17":4951,"30S ribosomal protein S9":4951,"transcription factor activity, sequence-specific DNA binding":4940,"30S ribosomal protein S19":4938,"30S ribosomal protein S12":4934,"DNA repair":4921,"T cell receptor signaling pathway":4878,"30S ribosomal protein S20":4875,"regulation of transcription, DNA-templated":4858,"30S ribosomal protein S8":4851,"CHAPERONE":4831,"Gag-Pol polyprotein":4819,"30S ribosomal protein S15":4794,"Proteasome subunit beta type-1":4790,"protease binding":4782,"Baker's yeast":4768,"ATP + H(2)O = ADP + phosphate.":4767,"-!- Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication. -!- To perform this task the enzyme combines two distinct activities. -!- The polymerase domain (EC 2.7.7.49) occupies the N-terminal two- thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third. -!- The RNase H domain of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites.":4758,"-!- This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13.":4758,"3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.":4758,"Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.":4758,"Exoribonuclease H.":4758,"Retroviral ribonuclease H.":4758,"platelet degranulation":4747,"G2/M transition of mitotic cell cycle":4741,"Proteasome subunit alpha type-3":4738,"Proteasome subunit beta type-4":4727,"Proteasome subunit alpha type-5":4726,"Proteasome subunit beta type-2":4725,"Proteasome subunit alpha type-1":4724,"Proteasome subunit alpha type-2":4724,"Proteasome subunit alpha type-6":4724,"Proteasome subunit alpha type-4":4723,"Proteasome subunit beta type-3":4723,"endosome membrane":4718,"NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE":4680,"dendrite":4676,"Proteasome subunit beta type-7":4667,"Proteasome subunit beta type-6":4666,"Proteasome subunit beta type-5":4639,"phosphatidylinositol-mediated signaling":4610,"endopeptidase activity":4579,"Arabidopsis thaliana":4578,"interferon-gamma-mediated signaling pathway":4563,"positive regulation of apoptotic process":4556,"PYRIDOXAL-5'-PHOSPHATE":4545,"-!- Present in human immunodeficiency virus type 1. -!- Contributes to the maturation of the viral particle, and is a target of antiviral drugs. -!- Active enzyme is a dimer of identical 11-kDa subunits. -!- Similar enzymes occur in other retroviruses. -!- Belongs to peptidase family A2.":4543,"HIV-1 retropepsin.":4543,"Human immunodeficiency virus type 1 protease.":4543,"Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.":4543,"proteasome storage granule":4543,"GUANOSINE-5'-DIPHOSPHATE":4539,"platelet activation":4519,"DNA-directed DNA polymerase activity":4516,"Human immunodeficiency virus 1":4499,"peptidyl-serine phosphorylation":4484,"Hydrolase":4453,"Rattus":4429,"response to hypoxia":4413,"baker's yeast":4388,"phagocytic vesicle membrane":4383,"response to heat":4379,"Saccharomyces":4375,"Bacillus subtilis":4364,"TETRAETHYLENE GLYCOL":4357,"ESCHERICHIA COLI":4335,"synapse":4303,"TRANSFERASE/DNA":4302,"Norway rat":4297,"50S ribosomal protein L2":4294,"50S ribosomal protein L3":4281,"Probable proteasome subunit alpha type-7":4273,"NICKEL (II) ION":4264,"50S ribosomal protein L6":4239,"oxidation-reduction process":4232,"50S ribosomal protein L15":4214,"50S ribosomal protein L30":4209,"negative regulation of gene expression":4197,"SUGAR (4-MER)":4186,"establishment of protein localization":4175,"50S ribosomal protein L5":4166,"50S ribosomal protein L23":4165,"50S ribosomal protein L18":4164,"50S ribosomal protein L14":4163,"50S ribosomal protein L13":4153,"50S ribosomal protein L29":4153,"50S ribosomal protein L22":4152,"50S ribosomal protein L4":4150,"positive regulation of ERK1 and ERK2 cascade":4139,"2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL":4135,"protein phosphatase binding":4132,"50S ribosomal protein L24":4122,"intracellular signal transduction":4115,"Ras protein signal transduction":4091,"regulation of transcription from RNA polymerase II promoter":4074,"Salmonella enterica subsp. enterica serovar Typhimurium str. LT2":4070,"STRUCTURAL PROTEIN":4044,"tertiary granule lumen":4042,"50S ribosomal protein L17":4038,"50S ribosomal protein L16":4034,"membrane organization":4029,"50S ribosomal protein L20":4028,"50S ribosomal protein L25":4026,"50S ribosomal protein L27":4022,"50S ribosomal protein L32":4015,"50S ribosomal protein L19":4014,"50S ribosomal protein L35":4013,"antigen processing and presentation of peptide antigen via MHC class I":4012,"50S ribosomal protein L21":4011,"50S ribosomal protein L34":4010,"apoptotic process":3999,"early endosome membrane":3986,"response to drug":3970,"antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent":3964,"CELL ADHESION":3957,"T cell costimulation":3947,"antimicrobial humoral immune response mediated by antimicrobial peptide":3942,"transcription initiation from RNA polymerase II promoter":3921,"50S ribosomal protein L28":3911,"50S ribosomal protein L33":3905,"proteasome core complex, alpha-subunit complex":3901,"DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest":3900,"glycoprotein binding":3897,"ER to Golgi transport vesicle membrane":3893,"SUGAR BINDING PROTEIN":3890,"manganese ion binding":3849,"Ras guanyl-nucleotide exchange factor activity":3826,"positive regulation of I-kappaB kinase/NF-kappaB signaling":3826,"protein C-terminus binding":3823,"receptor-mediated endocytosis":3814,"METAL BINDING PROTEIN":3808,"proteasome core complex, beta-subunit complex":3802,"azurophil granule lumen":3794,"activation of MAPK activity":3791,"protein homotetramerization":3789,"extracellular matrix":3752,"Sus scrofa":3742,"cellular response to oxidative stress":3741,"cellular response to lipopolysaccharide":3736,"growth":3722,"ELECTRON TRANSPORT":3699,"protein folding":3674,"neuronal cell body":3670,"protein homooligomerization":3670,"Fc-gamma receptor signaling pathway involved in phagocytosis":3669,"Transferase":3666,"FORMIC ACID":3657,"extracellular matrix organization":3656,"mitochondrial outer membrane":3650,"postsynaptic density":3635,"16S rRNA":3631,"stimulatory C-type lectin receptor signaling pathway":3627,"PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER":3605,"K-12":3596,"4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID":3590,"Thermus":3588,"retina homeostasis":3571,"chaperone binding":3570,"Genome polyprotein":3568,"Thermotoga maritima":3555,"FE (II) ION":3554,"TRIETHYLENE GLYCOL":3542,"regulation of complement activation":3541,"Drosophila melanogaster":3536,"FLAVIN MONONUCLEOTIDE":3533,"ATCC 204508 / S288c":3524,"ER to Golgi vesicle-mediated transport":3516,"flavin adenine dinucleotide binding":3500,"ATPase binding":3485,"defense response to bacterium":3481,"nitric oxide biosynthetic process":3476,"ion channel binding":3468,"peptidyl-tyrosine phosphorylation":3466,"regulation of apoptotic process":3453,"-!- Cf. EC 3.2.1.14.":3448,"Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl- D-glucosamine residues in chitodextrins.":3448,"Lysozyme.":3448,"Muramidase.":3448,"cell wall":3439,"30S ribosomal protein S14":3437,"vascular endothelial growth factor receptor signaling pathway":3434,"50S ribosomal protein L9":3432,"inflammatory response":3432,"phosphatidylinositol-4,5-bisphosphate 3-kinase activity":3413,"vesicle":3406,"ACETIC ACID":3395,"electron carrier activity":3386,"defense response to Gram-positive bacterium":3374,"UNKNOWN FUNCTION":3367,"-!- Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- See also EC 2.7.7.6.":3360,"RNA nucleotidyltransferase (RNA-directed).":3360,"RNA-directed RNA polymerase.":3360,"antibacterial humoral response":3356,"external side of plasma membrane":3356,"receptor complex":3351,"regulation of phosphatidylinositol 3-kinase signaling":3348,"lysozyme activity":3326,"Oxidoreductase":3323,"sequence-specific DNA binding":3322,"TOXIN":3314,"HB8":3312,"drug binding":3310,"integral component of lumenal side of endoplasmic reticulum membrane":3304,"nitric-oxide synthase activity":3299,"positive regulation of protein kinase B signaling":3283,"virion assembly":3273,"membrane raft":3266,"nuclear speck":3254,"response to lipopolysaccharide":3245,"late endosome":3242,"DNA BINDING PROTEIN":3238,"integral component of membrane":3220,"arginine catabolic process":3207,"specific granule lumen":3205,"recycling endosome membrane":3190,"positive regulation of NF-kappaB transcription factor activity":3183,"-!- Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain. -!- In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families. -!- Formerly EC 2.7.1.112.":3173,"Cytoplasmic protein tyrosine kinase.":3173,"Non-specific protein-tyrosine kinase.":3173,"intracellular":3141,"DNA replication":3139,"hydrolase":3132,"-!- The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans. -!- In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies. -!- Formerly EC 2.7.1.112.":3121,"Receptor protein tyrosine kinase.":3121,"Receptor protein-tyrosine kinase.":3121,"Geobacillus stearothermophilus":3116,"Oryctolagus cuniculus":3103,"regulation of defense response to virus by virus":3102,"SUGAR (5-MER)":3101,"Pseudomonas":3096,"heparin binding":3076,"platelet alpha granule lumen":3074,"ERBB2 signaling pathway":3062,"Nucleic acid-binding proteins":3049,"multicellular organism development":3035,"31-meric":3031,"protein polyubiquitination":3003,"response to oxidative stress":2997,"-!- This eukaryotic enzyme, which is found in plants and animals, consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain. -!- Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. -!- May produce superoxide under certain conditions. -!- Cf. EC 1.14.13.165.":2986,"2 L-arginine + 3 NADPH + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O.":2986,"Endothelium-derived relaxation factor-forming enzyme. Endothelium-derived relaxing factor synthase. NADPH-diaphorase. Nitric-oxide synthetase. NO synthase.":2986,"Nitric-oxide synthase (NADPH).":2986,"cell adhesion":2986,"calmodulin binding":2981,"Pyrococcus horikoshii OT3":2980,"50S ribosomal protein L36":2976,"Sulfolobus solfataricus P2":2969,"CITRIC ACID":2966,"cellular response to mechanical stimulus":2960,"axon guidance":2956,"antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent":2953,"GTP binding":2932,"serine-type peptidase activity":2920,"nuclear membrane":2913,"copper ion binding":2893,"chemotaxis":2883,"NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE":2877,"nuclear chromatin":2877,"Hemagglutinin":2867,"protein tetramerization":2860,"unfolded protein binding":2837,"response to estrogen":2835,"N-ACETYL-D-GLUCOSAMINE":2830,"BETA-MERCAPTOETHANOL":2825,"S-ADENOSYL-L-HOMOCYSTEINE":2815,"ubiquitin-protein transferase activity":2807,"base-excision repair":2800,"OSMIUM (III) HEXAMMINE":2794,"negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle":2794,"bicarbonate transport":2777,"GTPase activity":2767,"outer membrane-bounded periplasmic space":2750,"early endosome":2730,"p53 binding":2709,"positive regulation of reactive oxygen species metabolic process":2707,"ephrin receptor signaling pathway":2704,"Golgi lumen":2693,"5,6,7,8-TETRAHYDROBIOPTERIN":2682,"FMN binding":2674,"Lentivirus":2672,"21-meric":2663,"fibrinolysis":2659,"positive regulation of canonical Wnt signaling pathway":2657,"TRANSLATION, RIBOSOME, 40S, 60S, 80S, EUKARYOTE, RNA-PROTEIN COMPLEX, INHIBITOR, ANTIBIOTIC":2652,"immune response":2649,"positive regulation of MAP kinase activity":2638,"-!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase).":2633,"RNA helicase.":2633,"G-protein coupled receptor signaling pathway":2632,"translesion synthesis":2632,"Pseudomonas putida":2626,"GUANOSINE-5'-TRIPHOSPHATE":2623,"Haloarcula marismortui ATCC 43049":2621,"receptor activity":2614,"epidermal growth factor receptor signaling pathway":2612,"type I interferon signaling pathway":2611,"z-form double helix":2604,"transcription regulatory region DNA binding":2593,"5S ribosomal RNA":2586,"peroxisome":2582,"Bacillus anthracis":2581,"G1/S transition of mitotic cell cycle":2580,"NADP binding":2575,"aging":2574,"iron ion binding":2573,"Influenza A virus":2570,"positive regulation of sequence-specific DNA binding transcription factor activity":2570,"response to wounding":2567,"RNA BINDING PROTEIN":2563,"defense response to Gram-negative bacterium":2561,"-!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized. -!- See also EC 2.7.7.19 and EC 2.7.7.48.":2553,"DNA-dependent RNA polymerase. RNA nucleotidyltransferase (DNA-directed). RNA polymerase I. RNA polymerase II. RNA polymerase III.":2553,"DNA-directed RNA polymerase.":2553,"tumor necrosis factor-mediated signaling pathway":2549,"pyridoxal phosphate binding":2547,"sarcolemma":2542,"PENTAETHYLENE GLYCOL":2538,"microtubule binding":2537,"CELL CYCLE":2536,"protein N-terminus binding":2535,"scaffold protein binding":2533,"ADENOSINE MONOPHOSPHATE":2526,"positive regulation of T cell cytokine production":2526,"regulation of mRNA stability":2525,"disordered domain specific binding":2514,"regulation of transcription from RNA polymerase II promoter in response to hypoxia":2510,"Archaeoglobus fulgidus DSM 4304":2505,"heptameric":2497,"lysosome":2497,"protein ubiquitination involved in ubiquitin-dependent protein catabolic process":2494,"RIBOSOME/ANTIBIOTIC":2493,"OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR":2490,"IODIDE ION":2484,"HIV-1":2483,"PROTEIN TRANSPORT":2475,"IMIDAZOLE":2467,"negative regulation of canonical Wnt signaling pathway":2467,"Pyrococcus":2465,"fibroblast growth factor receptor signaling pathway":2463,"platelet aggregation":2458,"50S ribosomal protein L11":2457,"response to organic cyclic compound":2457,"cattle":2455,"nuclear body":2454,"Bos":2445,"viral life cycle":2444,"P-loop containing nucleotide triphosphate hydrolases":2438,"regulation of cellular response to heat":2433,"positive regulation of T cell mediated cytotoxicity":2429,"blood coagulation, intrinsic pathway":2428,"antigen processing and presentation of endogenous peptide antigen via MHC class I":2424,"protein stabilization":2420,"lysosomal membrane":2415,"positive regulation of protein binding":2413,"Pyrococcus horikoshii":2410,"signal peptide processing":2402,"UNKNOWN ATOM OR ION":2399,"mitochondrial intermembrane space":2397,"cell migration":2388,"S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.":2387,"chemical synaptic transmission":2386,"peptidyl-threonine phosphorylation":2386,"apical part of cell":2384,"protein complex assembly":2378,"dendritic spine":2368,"response to ethanol":2356,"activation of cysteine-type endopeptidase activity involved in apoptotic process":2350,"Immunoglobulins":2337,"Serine endopeptidases.":2328,"trans-Golgi network":2294,"growth factor activity":2293,"phosphoprotein binding":2291,"amino acid binding":2290,"30S RIBOSOMAL PROTEIN S11":2287,"30S RIBOSOMAL PROTEIN S15":2286,"30S RIBOSOMAL PROTEIN S6":2283,"30S RIBOSOMAL PROTEIN S18":2276,"Aquifex aeolicus VF5":2274,"30S RIBOSOMAL PROTEIN S19":2273,"actin cytoskeleton":2272,"30S RIBOSOMAL PROTEIN S12":2270,"30S RIBOSOMAL PROTEIN S10":2269,"30S RIBOSOMAL PROTEIN S13":2269,"30S RIBOSOMAL PROTEIN S16":2269,"30S RIBOSOMAL PROTEIN S17":2269,"30S RIBOSOMAL PROTEIN S20":2269,"30S RIBOSOMAL PROTEIN S3":2269,"30S RIBOSOMAL PROTEIN S4":2269,"30S RIBOSOMAL PROTEIN S5":2269,"30S RIBOSOMAL PROTEIN S7":2269,"30S RIBOSOMAL PROTEIN S8":2269,"30S RIBOSOMAL PROTEIN S9":2269,"30S RIBOSOMAL PROTEIN S2":2268,"complement activation":2267,"-!- The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. -!- Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD. -!- The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.":2263,"NTP + H(2)O = NDP + phosphate.":2263,"NTPase. Nucleoside 5-triphosphatase. Nucleoside triphosphate hydrolase. Nucleoside triphosphate phosphohydrolase. Nucleoside-5-triphosphate phosphohydrolase. Nucleoside-triphosphatase.":2263,"Nucleoside-triphosphate phosphatase.":2263,"hydrogen peroxide catabolic process":2259,"hexadecameric":2258,"protein-DNA complex":2256,"positive regulation of cell growth":2249,"COENZYME A":2248,"peptidyl-glutamic acid carboxylation":2241,"COBALT (II) ION":2240,"-!- A group of enzymes of broad specificity. -!- R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. -!- Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. -!- Formerly EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7.":2239,"Glutathione S-alkyltransferase. Glutathione S-aralkyltransferase. Glutathione S-aryltransferase. S-(hydroxyalkyl)glutathione lyase.":2239,"Glutathione transferase.":2239,"RX + glutathione = HX + R-S-glutathione.":2239,"30S ribosomal protein S21":2236,"pathogenesis":2228,"H37Rv":2222,"MUS MUSCULUS":2207,"DNA-directed RNA polymerase II, core complex":2206,"peptide antigen binding":2204,"cell cycle arrest":2202,"Mycobacterium":2193,"HEME C":2191,"cell-cell signaling":2184,"transferase":2184,"Pyrococcus furiosus DSM 3638":2175,"Plasmodium falciparum":2169,"Wnt signaling pathway":2166,"terminal bouton":2159,"-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.":2156,"RING E3 ligase. Ubiquitin transferase RING E3.":2156,"RING-type E3 ubiquitin transferase.":2156,"response to antibiotic":2156,"transcription, DNA-templated":2147,"30S RIBOSOMAL PROTEIN THX":2145,"Lysozyme C":2143,"Enterobacteria phage T4":2138,"positive regulation of neuron death":2138,"anaphase-promoting complex-dependent catabolic process":2134,"positive regulation of receptor-mediated endocytosis":2133,"30-meric":2132,"female pregnancy":2131,"Methanocaldococcus jannaschii DSM 2661":2128,"endocytic vesicle membrane":2128,"Thermotoga":2126,"protein self-association":2125,"integrin binding":2123,"RNA polymerase II core promoter proximal region sequence-specific DNA binding":2118,"transcription coactivator activity":2115,"protein complex binding":2111,"50S ribosomal protein L31":2106,"negative regulation of extrinsic apoptotic signaling pathway via death domain receptors":2104,"FE3-S4 CLUSTER":2088,"transforming growth factor beta receptor signaling pathway":2088,"-!- Zinc is only requires in class-B enzymes. -!- A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. -!- Formerly EC 3.5.2.8.":2085,"A beta-lactam + H(2)O = a substituted beta-amino acid.":2085,"Beta-lactamase.":2085,"Cephalosporinase. Penicillinase.":2085,"oxidoreductase":2081,"extracellular matrix disassembly":2077,"midbody":2062,"regulation of cell proliferation":2062,"Salmonella typhimurium":2055,"Cysteine endopeptidases.":2053,"error-free translesion synthesis":2053,"mRNA binding":2048,"negative regulation of cysteine-type endopeptidase activity involved in apoptotic process":2042,"mRNA splicing, via spliceosome":2041,"NITRATE ION":2040,"microtubule":2033,"movement of cell or subcellular component":2031,"fusion of virus membrane with host plasma membrane":2030,"beta-catenin binding":2029,"rat":2028,"tetradecameric":2028,"METAL TRANSPORT":2021,"transport":2019,"positive regulation of peptidyl-serine phosphorylation":2018,"SUGAR (6-MER)":2004,"aspartic-type endopeptidase activity":2004,"neuron projection":2004,"Other carbon-oxygen lyases.":1990,"mitotic cell cycle":1983,"32-meric":1982,"macroautophagy":1982,"DNA-dependent DNA replication":1981,"response to hydrogen peroxide":1981,"50S ribosomal protein L21e":1980,"50S ribosomal protein L37e":1980,"50S ribosomal protein L39e":1980,"negative regulation of sequence-specific DNA binding transcription factor activity":1973,"nuclear chromosome, telomeric region":1970,"protein refolding":1969,"positive regulation of peptidyl-tyrosine phosphorylation":1968,"UNKNOWN LIGAND":1966,"1-phosphatidylinositol-3-kinase activity":1961,"double-strand break repair":1959,"50S ribosomal protein L13P":1955,"50S ribosomal protein L23P":1954,"50S ribosomal protein L24P":1954,"50S ribosomal protein L29P":1954,"50S ribosomal protein L14P":1953,"50S ribosomal protein L15P":1953,"50S ribosomal protein L18P":1953,"50S ribosomal protein L22P":1953,"50S ribosomal protein L30P":1953,"50S ribosomal protein L3P":1953,"50S ribosomal protein L5P":1953,"50S ribosomal protein L6P":1953,"50S ribosomal protein L2P":1952,"non-membrane spanning protein tyrosine kinase activity":1945,"response to peptide hormone":1942,"response to activity":1941,"transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding":1937,"peptidyl-cysteine S-nitrosylation":1935,"dendrite cytoplasm":1929,"cellular response to epinephrine stimulus":1926,"5S RIBOSOMAL RNA":1924,"50S ribosomal protein L18e":1912,"axon":1909,"beta-amyloid binding":1909,"transmembrane transport":1908,"response to nicotine":1903,"23S rRNA":1895,"5S rRNA":1894,"histone deacetylase binding":1893,"multivesicular body":1893,"With NAD(+) or NADP(+) as acceptor.":1891,"Plasmodium falciparum 3D7":1885,"regulation of sensory perception of pain":1885,"periplasmic space":1883,"cellular response to iron ion":1881,"damaged DNA binding":1878,"50S ribosomal protein L44E":1877,"50S ribosomal protein L31e":1875,"HYDROLASE/DNA":1875,"serine protease inhibitor complex":1869,"B2M, CDABP0092, HDCMA22P":1867,"Bacteroides thetaiotaomicron VPI-5482":1866,"metal ion binding":1865,"nonameric":1865,"yeast":1861,"Aquifex aeolicus":1860,"perikaryon":1856,"PDZ domain binding":1855,"response to organonitrogen compound":1853,"cyclin-dependent protein kinase holoenzyme complex":1851,"ISOPROPYL ALCOHOL":1850,"entry into host cell":1850,"positive regulation of angiogenesis":1850,"TRANSCRIPTION/DNA":1848,"Sulfolobus solfataricus":1845,"HFE-transferrin receptor complex":1844,"mitochondrial inner membrane":1842,"transcription-coupled nucleotide-excision repair":1838,"Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.":1837,"beta-amyloid metabolic process":1836,"23S ribosomal RNA":1833,"mitochondrion organization":1833,"regulation of sequence-specific DNA binding transcription factor activity":1832,"-!- Belongs to peptidase family S1. -!- Formerly EC 3.4.4.4.":1830,"Alpha-trypsin. Beta-trypsin.":1830,"Trypsin.":1830,"endocytic vesicle lumen":1826,"VIRUS":1825,"DNA polymerase":1822,"cytoplasmic vesicle":1820,"FAD binding":1819,"protein heterotetramerization":1813,"receptor internalization":1804,"histone binding":1800,"-!- The enzyme catalyzes the reversible hydration of gaseous CO(2) to carbonic acid, which spontaneously converts to hydrogencarbonate under neutral pH. -!- It is widespread and found in archaea, bacteria, and eukaryotes. -!- Three distinct classes exist, and appear to have evolved independently.":1799,"Carbonate dehydratase. Carbonate hydro-lyase. Carbonic dehydratase.":1799,"Carbonic anhydrase.":1799,"H(2)CO(3) = CO(2) + H(2)O.":1799,"positive regulation of MAPK cascade":1797,"30S ribosomal protein Thx":1796,"PAROMOMYCIN":1794,"4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.":1790,"Ceruloplasmin. HEPH. Hephaestin.":1790,"Ferroxidase.":1790,"serpin family protein binding":1790,"negative regulation of epidermal growth factor receptor signaling pathway":1789,"lamellipodium":1787,"positive regulation of protein localization to nucleus":1781,"negative regulation of G2/M transition of mitotic cell cycle":1776,"double-stranded DNA binding":1774,"positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition":1774,"positive regulation of interferon-gamma production":1769,"positive regulation of cell death":1765,"SACCHAROMYCES CEREVISIAE":1762,"mitotic G1 DNA damage checkpoint":1761,"(4R)-2-METHYLPENTANE-2,4-DIOL":1757,"azurophil granule":1757,"uncoating of virus":1756,"negative regulation of protein binding":1755,"40S RIBOSOMAL PROTEIN S12":1753,"phospholipid binding":1752,"Methyltransferases.":1751,"gag-pol":1750,"establishment of integrated proviral latency":1749,"lipopolysaccharide binding":1749,"positive regulation of long-term synaptic potentiation":1749,"regulation of cell shape":1749,"60S RIBOSOMAL PROTEIN L32":1748,"TRANSLATION":1741,"angiogenesis":1739,"cellular response to starvation":1738,"signal transducer activity":1737,"regulation of heart contraction":1736,"Staphylococcus":1734,"cellular iron ion homeostasis":1734,"killing of cells of other organism":1734,"lysosomal lumen":1734,"response to vitamin E":1732,"histone phosphorylation":1730,"beta-N-acetylglucosaminidase activity":1725,"sodium channel regulator activity":1725,"Vibrio cholerae O1 biovar El Tor str. N16961":1724,"CITRATE ANION":1723,"CYTOPLASM":1723,"basolateral plasma membrane":1722,"calcium-dependent protein binding":1722,"cytoskeleton":1722,"apical plasma membrane":1720,"Human immunodeficiency virus type 1 BH10":1719,"response to lead ion":1716,"positive regulation of release of sequestered calcium ion into cytosol":1715,"regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle":1715,"cyclin A2-CDK2 complex":1711,"antigen processing and presentation of exogenous peptide antigen via MHC class II":1708,"50S ribosomal protein L37Ae":1706,"UBIQUITIN-60S RIBOSOMAL PROTEIN L40":1706,"negative regulation of peptidyl-serine phosphorylation":1706,"protein heterooligomerization":1706,"response to nitric oxide":1702,"vesicle membrane":1702,"RNA-directed DNA polymerase activity":1700,"NIK/NF-kappaB signaling":1699,"ionotropic glutamate receptor activity":1698,"25-meric":1696,"OT3":1696,"GLUTAMIC ACID":1695,"ephrin receptor binding":1695,"regulation of membrane depolarization":1695,"nuclear envelope":1693,"Nitric oxide synthase, brain":1691,"photoreceptor inner segment":1687,"-!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase).":1684,"DNA helicase.":1684,"cadmium ion binding":1684,"-!- Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. -!- It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation. -!- Formerly EC 2.7.1.37.":1680,"Cdc2 kinase. Cdk-activating kinase. Cdk-activating protein kinase.":1680,"Cyclin-dependent kinase.":1680,"nitric oxide mediated signal transduction":1680,"Streptomyces":1678,"negative regulation of blood pressure":1675,"negative regulation of proteolysis":1675,"23-meric":1674,"proteolysis involved in cellular protein catabolic process":1672,"Oxidoreductases.":1670,"cellular response to hypoxia":1669,"early endosome lumen":1669,"actin filament binding":1668,"spindle microtubule":1666,"xenobiotic metabolic process":1664,"MHC class II protein complex binding":1662,"Caenorhabditis elegans":1659,"structural genomics, unknown function":1659,"response to nutrient levels":1658,"carbonate dehydratase activity":1657,"positive regulation of receptor binding":1657,"GLUTATHIONE":1647,"Putative uncharacterized protein":1646,"double-strand break repair via nonhomologous end joining":1644,"DODECYL-BETA-D-MALTOSIDE":1643,"negative regulation of insulin secretion":1639,"Wnt signaling pathway, planar cell polarity pathway":1634,"-!- Some enzymes in this group hydrolyze alpha-L-arabinosides; some animal enzymes also hydrolyze beta-D-fucosides and beta-D-glucosides (cf. EC 3.2.1.108).":1633,"Beta-galactosidase.":1633,"Exo-(1->4)-beta-D-galactanase. Lactase.":1633,"Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D- galactosides.":1633,"positive regulation of blood vessel diameter":1632,"Streptococcus pneumoniae TIGR4":1627,"membrane protein ectodomain proteolysis":1627,"60S RIBOSOMAL PROTEIN L30":1626,"60S RIBOSOMAL PROTEIN L39":1626,"transmembrane receptor protein tyrosine kinase activity":1626,"CARDIOLIPIN":1625,"60S RIBOSOMAL PROTEIN L28":1623,"60S RIBOSOMAL PROTEIN L29":1623,"60S RIBOSOMAL PROTEIN L38":1623,"cyclin-dependent protein serine/threonine kinase activity":1623,"positive regulation of nitric oxide biosynthetic process":1623,"60S RIBOSOMAL PROTEIN L17-A":1621,"60S RIBOSOMAL PROTEIN L25":1621,"60S RIBOSOMAL PROTEIN L26-A":1621,"60S RIBOSOMAL PROTEIN L31-A":1621,"60S RIBOSOMAL PROTEIN L24-A":1619,"60S RIBOSOMAL PROTEIN L15-A":1618,"60S RIBOSOMAL PROTEIN L16-A":1618,"60S RIBOSOMAL PROTEIN L21-A":1618,"60S RIBOSOMAL PROTEIN L22-A":1618,"60S RIBOSOMAL PROTEIN L23-A":1618,"60S RIBOSOMAL PROTEIN L27-A":1618,"60S RIBOSOMAL PROTEIN L33-A":1618,"60S RIBOSOMAL PROTEIN L34-A":1618,"60S RIBOSOMAL PROTEIN L36-A":1618,"60S RIBOSOMAL PROTEIN L37-A":1618,"60S RIBOSOMAL PROTEIN L42-A":1618,"60S RIBOSOMAL PROTEIN L18-A":1617,"Beta-galactosidase":1617,"behavioral response to cocaine":1617,"60S RIBOSOMAL PROTEIN L20-A":1616,"60S RIBOSOMAL PROTEIN L35-A":1616,"60S RIBOSOMAL PROTEIN L41-A":1616,"60S RIBOSOMAL PROTEIN L43-A":1616,"60S RIBOSOMAL PROTEIN L19-A":1615,"cellular response to insulin stimulus":1615,"CARBONATE ION":1614,"entry of bacterium into host cell":1614,"apoptotic signaling pathway":1613,"negative regulation of receptor binding":1612,"PAO1":1610,"single-stranded DNA binding":1608,"-!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.":1607,"Phosphotyrosine phosphatase. PTPase.":1607,"Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.":1607,"Protein-tyrosine-phosphatase.":1607,"negative regulation of cytosolic calcium ion concentration":1607,"positive regulation of blood coagulation":1607,"negative regulation of fibrinolysis":1602,"negative regulation of heart contraction":1601,"positive regulation of sodium ion transmembrane transport":1596,"RNA-dependent DNA biosynthetic process":1595,"negative regulation of vasoconstriction":1594,"Streptococcus pneumoniae":1593,"T cell activation":1593,"cytoplasmic stress granule":1591,"23S RIBOSOMAL RNA":1589,"MYCOBACTERIUM TUBERCULOSIS":1588,"BAKER'S YEAST":1587,"BL21":1586,"cellular response to nitric oxide":1585,"30S RIBOSOMAL PROTEIN S14":1582,"regulation of protein stability":1582,"Deinococcus radiodurans R1":1580,"positive regulation of ferrous iron binding":1580,"positive regulation of ferrous iron import across plasma membrane":1580,"positive regulation of transferrin receptor binding":1580,"brown rat,rat,rats":1577,"gluconeogenesis":1577,"toxic substance binding":1577,"Cryphonectria parasitica":1572,"T4-like viruses":1570,"DNA-(apurinic or apyrimidinic site) lyase activity":1566,"16S ribosomal RNA":1562,"glutathione transferase activity":1558,"nucleotide-excision repair, DNA incision":1558,"-!- From the ascomycete Endothia parasitica. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.10.":1557,"Endothia aspartic proteinase.":1557,"Endothiapepsin":1557,"Endothiapepsin.":1557,"Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.":1557,"Haemophilus influenzae Rd KW20":1556,"40S RIBOSOMAL PROTEIN S3":1555,"positive regulation of phosphatidylinositol 3-kinase signaling":1554,"nervous system development":1552,"40S RIBOSOMAL PROTEIN S13":1551,"Methanocaldococcus jannaschii":1551,"-!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.":1550,"40S RIBOSOMAL PROTEIN S15":1550,"40S RIBOSOMAL PROTEIN S2":1550,"40S RIBOSOMAL PROTEIN S20":1550,"40S RIBOSOMAL PROTEIN S5":1550,"Cyclophilin. Peptidyl-prolyl cis-trans isomerase. Peptidylprolyl cis-trans isomerase. PPIase. Rotamase.":1550,"Peptidylproline (omega=180) = peptidylproline (omega=0).":1550,"Peptidylprolyl isomerase.":1550,"Fruit fly":1547,"168":1546,"Archaeoglobus fulgidus":1544,"BROMIDE ION":1544,"cysteine-type endopeptidase activity":1543,"50S ribosomal protein L7Ae":1542,"DNA polymerase beta":1541,"MRNA":1540,"positive regulation of proteasomal ubiquitin-dependent protein catabolic process":1538,"kinase binding":1537,"cell wall macromolecule catabolic process":1536,"cell-matrix adhesion":1536,"HLA class I histocompatibility antigen, A-2 alpha chain":1529,"SUGAR (B-OCTYLGLUCOSIDE)":1526,"chicken":1524,"cytoskeletal protein binding":1524,"2 superoxide + 2 H(+) = O(2) + H(2)O(2).":1521,"Superoxide dismutase.":1521,"actin binding":1518,"centriole replication":1518,"metalloendopeptidase activity":1518,"cyclin binding":1516,"40S RIBOSOMAL PROTEIN S0-A":1515,"40S RIBOSOMAL PROTEIN S1-A":1515,"40S RIBOSOMAL PROTEIN S11-A":1515,"40S RIBOSOMAL PROTEIN S14-A":1515,"40S RIBOSOMAL PROTEIN S16-A":1515,"40S RIBOSOMAL PROTEIN S17-A":1515,"40S RIBOSOMAL PROTEIN S18-A":1515,"40S RIBOSOMAL PROTEIN S19-A":1515,"40S RIBOSOMAL PROTEIN S21-A":1515,"40S RIBOSOMAL PROTEIN S22-A":1515,"40S RIBOSOMAL PROTEIN S23-A":1515,"40S RIBOSOMAL PROTEIN S24-A":1515,"40S RIBOSOMAL PROTEIN S25-A":1515,"40S RIBOSOMAL PROTEIN S4-A":1515,"40S RIBOSOMAL PROTEIN S6-A":1515,"40S RIBOSOMAL PROTEIN S7-A":1515,"40S RIBOSOMAL PROTEIN S8-A":1515,"40S RIBOSOMAL PROTEIN S9-A":1515,"SCF-dependent proteasomal ubiquitin-dependent protein catabolic process":1515,"negative regulation of transforming growth factor beta receptor signaling pathway":1515,"-!- Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2 is necessary for enzyme activation. -!- Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline. -!- A distinguishing feature of all MAPKs is the conserved sequence Thr- Xaa-Tyr (TXY). -!- Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. -!- Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury. -!- Formerly EC 2.7.1.37.":1513,"C-Jun N-terminal kinase. ERK. Extracellular signal-regulated kinase. JNK. MAP kinase. MAPK. MBP kinase I. MBP kinase II. Microtubule-associated protein 2 kinase. Microtubule-associated protein kinase. Myelin basic protein kinase. SAPK. Stress-activated protein kinase.":1513,"Mitogen-activated protein kinase.":1513,"3'-5' exonuclease activity":1511,"eicosameric":1511,"BIOSYNTHETIC PROTEIN":1510,"RNA-DNA hybrid ribonuclease activity":1509,"30S ribosomal protein S14 type Z":1508,"carbohydrate metabolic process":1508,"phosphorylation":1505,"fatty acid binding":1501,"regulation of cytosolic calcium ion concentration":1500,"Pyrococcus furiosus":1498,"Helicobacter pylori":1494,"beta-aspartyl-peptidase activity":1494,"-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.":1493,"Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).":1493,"Ubiquitin C-terminal hydrolase. Ubiquitin carboxyl-terminal hydrolase. Ubiquitin thiolesterase.":1493,"Ubiquitinyl hydrolase 1.":1493,"meiotic cell cycle":1493,"Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu- Phe in the Swedish variant of Alzheimer's amyloid precursor protein.":1492,"Salmonella":1489,"NAD binding":1486,"peptide binding":1486,"regulation of blood pressure":1486,"viral genome packaging":1483,"Cajal body":1479,"Geobacillus":1478,"regulation of gene silencing":1478,"positive regulation of DNA replication":1475,"negative regulation of cell growth":1474,"tridecameric":1474,"ciliary basal body docking":1473,"I-kappaB kinase/NF-kappaB signaling":1467,"PRE2, DOA3, PRG1, YPR103W, P8283.10":1467,"HEXAETHYLENE GLYCOL":1466,"integrin-mediated signaling pathway":1465,"negative regulation of protein catabolic process":1463,"ubiquitin binding":1463,"Prothrombin":1462,"actin cytoskeleton organization":1458,"ionotropic glutamate receptor complex":1455,"base-excision repair, DNA ligation":1454,"antigen binding":1453,"catabolism by organism of cell wall peptidoglycan in other organism":1453,"Beta-secretase 1":1450,"Rhodobacter sphaeroides":1450,"positive regulation of GTPase activity":1450,"negative regulation of extrinsic apoptotic signaling pathway":1447,"cellular response to vascular endothelial growth factor stimulus":1446,"RATTUS NORVEGICUS":1445,"MALONATE ION":1443,"-!- More selective than trypsin and plasmin. -!- Belongs to peptidase family S1. -!- Formerly EC 3.4.4.13.":1442,"Fibrinogenase.":1442,"Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.":1442,"Thrombin.":1442,"P-body":1441,"PHOTOSYNTHESIS":1440,"cell-cell junction":1440,"lyase activity":1440,"nucleotide-excision repair, DNA incision, 5'-to lesion":1440,"Exodeoxyribonucleases producing 5'-phosphomonoesters.":1439,"H37RV":1439,"intracellular ribonucleoprotein complex":1439,"protein dephosphorylation":1438,"Histone H4":1437,"STRONTIUM ION":1437,"-!- Suggested to be the major 'beta-secretase' responsible for the cleavage of the beta-amyloid precursor protein to form the amyloidogenic beta-peptide that is implicated in the pathology of Alzheimer's disease. -!- Belongs to peptidase family A1.":1436,"BACE1. Beta-secretase. Beta-site Alzheimer's amyloid precursor protein cleaving enzyme 1. Beta-site APP-cleaving enzyme 1. Membrane-associated aspartic protease 2.":1436,"Golgi-associated vesicle lumen":1436,"Memapsin 2.":1436,"positive regulation of endothelial cell proliferation":1436,"regulation of nitric-oxide synthase activity":1434,"T cell receptor binding":1433,"cellular response to cadmium ion":1433,"global genome nucleotide-excision repair":1432,"spindle":1431,"autophagy":1430,"base-excision repair, base-free sugar-phosphate removal":1430,"toll-like receptor signaling pathway":1430,"cellular response to estradiol stimulus":1429,"chloroplast":1427,"40S RIBOSOMAL PROTEIN S10-A":1426,"cell adhesion molecule binding":1426,"Carbonic anhydrase 2":1422,"Methanothermobacter thermautotrophicus str. Delta H":1422,"Cationic trypsin":1421,"drug transmembrane transporter activity":1420,"nucleotide binding":1412,"GDP binding":1411,"Helicobacter pylori 26695":1410,"Cyclin-dependent kinase 2":1406,"Mycobacterium smegmatis str. MC2 155":1406,"RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding":1406,"Xenopus laevis":1404,"negative regulation of protein kinase activity":1403,"positive regulation of endothelial cell migration":1401,"Schizosaccharomyces pombe 972h-":1400,"positive regulation of muscle cell differentiation":1399,"protein ADP-ribosylation":1399,"regulation of tumor necrosis factor-mediated signaling pathway":1399,"PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER":1395,"URIDINE-5'-DIPHOSPHATE":1395,"Endolysin":1394,"PML body":1392,"regulation of inflammatory response":1391,"cellular response to reactive oxygen species":1386,"positive regulation of collagen biosynthetic process":1385,"response to nutrient":1384,"negative regulation of neuron projection development":1381,"kainate selective glutamate receptor activity":1378,"negative regulation of platelet activation":1375,"response to virus":1374,"ferrous iron binding":1368,"regulation of cell motility":1368,"centrosome duplication":1366,"regulation of lipid metabolic process":1366,"MERCURY (II) ION":1365,"cytokine activity":1365,"nucleotide-excision repair":1365,"cellular response to gamma radiation":1364,"ubiquitin protein ligase activity":1363,"HA":1361,"beta-galactosidase activity":1361,"cyclin-dependent protein kinase activity":1361,"carbohydrate binding":1360,"cellular response to drug":1359,"neutrophil chemotaxis":1357,"positive regulation of phosphorylation":1353,"Enterobacteria phage T4 sensu lato":1351,"arylesterase activity":1349,"regulation of blood coagulation":1348,"regulation of cell adhesion mediated by integrin":1348,"Proteasome component PUP2":1346,"neutrophil mediated killing of gram-negative bacterium":1346,"animal organ morphogenesis":1345,"response to calcium ion":1345,"Viral protein":1344,"dendritic shaft":1342,"retinoid metabolic process":1342,"Mouse":1341,"Proteasome component C1":1339,"Proteasome component C11":1339,"Proteasome component C7-alpha":1339,"Proteasome component PRE5":1339,"Proteasome component PRE6":1339,"Proteasome component PUP3":1339,"Proteasome component Y13":1339,"Proteasome component Y7":1339,"cellular response to ionizing radiation":1339,"pentadecameric":1339,"methylated histone binding":1337,"negative regulation of cytokine production involved in inflammatory response":1333,"defense response to virus":1332,"glycolytic process":1332,"cell junction":1331,"double-strand break repair via homologous recombination":1327,"L(+)-TARTARIC ACID":1326,"":1324,"RNA polymerase II regulatory region sequence-specific DNA binding":1324,"angiotensin-activated signaling pathway":1323,"nuclear transport":1322,"HIV-1 M:B_HXB2R":1321,"regulation of anion transport":1320,"double-stranded RNA binding":1318,"negative regulation of type I interferon production":1315,"execution phase of apoptosis":1314,"phosphotyrosine binding":1314,"Proteasome component PRE2":1310,"Proteasome component PRE3":1310,"Proteasome component PRE4":1310,"Proteasome component PUP1":1310,"presynaptic membrane":1310,"DNA-directed RNA polymerase II subunit RPB2":1309,"cellular response to hydrogen peroxide":1309,"skeletal muscle myofibril":1308,"stress-activated MAPK cascade":1308,"endocytic vesicle":1305,"proteasomal protein catabolic process":1303,"transmembrane signaling receptor activity":1303,"core promoter sequence-specific DNA binding":1300,"drug transmembrane transport":1300,"oxygen transport":1300,"thrombospondin receptor activity":1299,"antimicrobial humoral response":1296,"negative regulation of translation":1295,"mismatch repair":1294,"endoplasmic reticulum unfolded protein response":1287,"negative regulation of astrocyte differentiation":1287,"growth cone":1286,"Escherichia coli O157:H7":1284,"NAD+ ADP-ribosyltransferase activity":1283,"cytolysis by host of symbiont cells":1283,"error-prone translesion synthesis":1282,"transcription regulatory region sequence-specific DNA binding":1282,"regulation of receptor recycling":1280,"JNK cascade":1279,"Notch signaling pathway":1278,"positive regulation of lipid kinase activity":1278,"positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway":1278,"endopeptidase activator activity":1275,"ion transmembrane transport":1273,"positive regulation of protein secretion":1271,"Vibrio cholerae":1270,"mRNA":1269,"Proteasome component C5":1267,"1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE":1263,"glucose homeostasis":1263,"protein homotrimerization":1263,"S-ADENOSYLMETHIONINE":1261,"PSEUDOMONAS AERUGINOSA":1257,"Beta-lactamase":1254,"HOUSE MOUSE":1252,"SUGAR (ALPHA-D-MANNOSE)":1252,"Staphylococcus aureus subsp. aureus Mu50":1251,"complement activation, classical pathway":1251,"nucleotide-excision repair, preincision complex assembly":1251,"collagen catabolic process":1248,"single-stranded RNA binding":1248,"TRANSCRIPTION REGULATOR":1247,"clathrin-coated vesicle membrane":1247,"Bacillus cereus":1246,"TAP binding":1246,"integrase activity":1246,"hemoglobin complex":1244,"intracellular transport of virus":1244,"APOPTOSIS":1242,"Sulfolobus":1241,"fibronectin binding":1241,"oxygen binding":1240,"bile acid and bile salt transport":1236,"chromatin remodeling":1233,"positive regulation of protein catabolic process":1233,"collagen binding":1232,"plasminogen activation":1232,"signal transduction in response to DNA damage":1232,"DNA-directed DNA polymerase":1229,"cell chemotaxis":1226,"\"winged helix\" repressor DNA binding domain":1225,"response to stress":1225,"Rat":1222,"Lyase":1221,"cell cortex":1221,"phosphatidylinositol biosynthetic process":1218,"proteasome complex":1218,"protein dimerization activity":1218,"substantia nigra development":1218,"Streptococcus":1217,"response to fungicide":1217,"Haemophilus influenzae":1213,"haptoglobin-hemoglobin complex":1213,"regulation of insulin secretion":1212,"Thermus aquaticus":1203,"circadian rhythm":1203,"transcription elongation from RNA polymerase II promoter":1203,"heat shock protein binding":1201,"positive regulation of protein complex assembly":1200,"MAP kinase activity":1199,"ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).":1197,"DNA-directed RNA polymerase II subunit RPB1":1197,"OXYGEN TRANSPORT":1194,"-!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34.":1193,"ATP synthase. Chloroplast ATPase. F(0)F(1)-ATPase. F(1)-ATPase. F(o)F(1)-ATPase. H(+)-transporting ATP synthase. H(+)-transporting ATPase. Mitochondrial ATPase.":1193,"H(+)-transporting two-sector ATPase.":1193,"Capsid protein":1192,"specific granule membrane":1192,"CACODYLATE ION":1190,"caveola":1190,"nucleobase-containing small molecule interconversion":1190,"phosphatidylinositol-4,5-bisphosphate binding":1189,"DNA-directed RNA polymerase II subunit RPB3":1185,"microtubule cytoskeleton":1185,"proteasome core complex assembly":1184,"-!- A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase. -!- The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. -!- Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21.":1183,"2 H(2)O(2) = O(2) + 2 H(2)O.":1183,"Catalase.":1183,"DNA-directed RNA polymerase II subunit RPB9":1183,"GENE REGULATION":1182,"50S ribosomal protein L10e":1178,"ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228":1178,"Endonucleolytic cleavage to 5'-phosphomonoester.":1178,"receptor tyrosine kinase binding":1178,"superoxide metabolic process":1178,"oxidoreductase activity":1177,"DNA BINDING PROTEIN/DNA":1176,"OXYGEN MOLECULE":1175,"MyD88-dependent toll-like receptor signaling pathway":1174,"DNA-directed RNA polymerases I, II, and III subunit RPABC1":1173,"Staphylococcus aureus subsp. aureus":1172,"peptidyl-tyrosine autophosphorylation":1172,"Gallus":1170,"ADP binding":1168,"NADPH binding":1164,"TRIF-dependent toll-like receptor signaling pathway":1163,"canonical glycolysis":1159,"50S ribosomal protein L19e":1158,"Mycobacterium tuberculosis CDC1551":1155,"positive regulation of telomerase activity":1155,"extracellular vesicle":1154,"CARBON MONOXIDE":1152,"SUGAR (7-MER)":1151,"intrinsic apoptotic signaling pathway in response to DNA damage":1151,"nuclear matrix":1151,"Transferase/DNA":1148,"MHC class I protein complex":1147,"Thermus thermophilus HB27":1146,"clathrin-coated endocytic vesicle membrane":1146,"Serum albumin":1143,"regulation of ERK1 and ERK2 cascade":1143,"Streptomyces coelicolor A3(2)":1139,"aminopeptidase activity":1139,"beta-2-microglobulin binding":1137,"synthetic construct":1137,"Hemoglobin subunit alpha":1135,"response to estradiol":1134,"Enterobacteria phage RB69":1131,"16S RRNA":1130,"Hemoglobin subunit beta":1130,"cellular amino acid biosynthetic process":1130,"cellular response to tumor necrosis factor":1129,"chaperone mediated protein folding requiring cofactor":1129,"SACCHAROMYCES CEREVISIAE CHROMOSOME XII COSMID 9634":1126,"negative regulation of I-kappaB kinase/NF-kappaB signaling":1125,"positive regulation of epithelial cell proliferation":1123,"alkali metal ion binding":1122,"beta-galactosidase complex":1122,"lactose catabolic process":1122,"With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors.":1120,"serine-type endopeptidase inhibitor activity":1119,"positive regulation of synaptic transmission":1117,"Trypanosoma brucei brucei":1116,"Yersinia pestis":1114,"RNA polymerase II transcription factor binding":1113,"Hsp90 protein binding":1112,"-!- Will utilize O(2) instead of CO(2), forming 3-phospho-D-glycerate and 2-phosphoglycolate.":1111,"2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O.":1111,"50S ribosomal protein L15e":1111,"Carboxydismutase. D-ribulose 1,5-diphosphate carboxylase. D-ribulose-1,5-bisphosphate carboxylase. Diphosphoribulose carboxylase. Ribulose 1,5-bisphosphate carboxylase. Ribulose 1,5-bisphosphate carboxylase/oxygenase. Ribulose 1,5-diphosphate carboxylase. Ribulose 1,5-diphosphate carboxylase/oxygenase. Ribulose bisphosphate carboxylase/oxygenase. Ribulose diphosphate carboxylase. Ribulose diphosphate carboxylase/oxygenase. RuBisCO. RuBP carboxylase.":1111,"Ribulose-bisphosphate carboxylase.":1111,"dephosphorylation":1111,"PYROPHOSPHATE 2-":1110,"-!- The enzyme does not act on 4-O-acetylated sialic acids. -!- An endo-alpha-sialidase activity is listed as EC 3.2.1.129. -!- See also EC 4.2.2.15.":1108,"AZIDE ION":1108,"Alpha-neuraminidase. N-acylneuraminate glycohydrolase. Neuraminidase. Sialidase.":1108,"DNA-directed RNA polymerases I, II, and III subunit RPABC2":1108,"Exo-alpha-sialidase.":1108,"Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.":1108,"nucleotide-excision repair, DNA duplex unwinding":1108,"DNA-directed RNA polymerases I, II, and III subunit RPABC3":1106,"DNA-directed RNA polymerases I, II, and III subunit RPABC4":1106,"DNA-directed RNA polymerases I, II, and III subunit RPABC5":1106,"antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent":1105,"37-meric":1104,"50S RIBOSOMAL PROTEIN L17":1103,"negative regulation of endothelial cell apoptotic process":1103,"fibrillar center":1102,"response to lithium ion":1101,"50S RIBOSOMAL PROTEIN L16":1100,"50S RIBOSOMAL PROTEIN L23":1100,"50S RIBOSOMAL PROTEIN L24":1100,"50S RIBOSOMAL PROTEIN L29":1100,"SH2 domain binding":1100,"50S RIBOSOMAL PROTEIN L25":1099,"FLUORESCENT PROTEIN":1099,"50S RIBOSOMAL PROTEIN L22":1098,"50S RIBOSOMAL PROTEIN L5":1098,"cellular response to UV":1098,"THIAMINE DIPHOSPHATE":1097,"extrinsic component of cytoplasmic side of plasma membrane":1097,"50S RIBOSOMAL PROTEIN L20":1096,"LT2":1096,"Multidrug efflux pump subunit AcrB":1096,"50S RIBOSOMAL PROTEIN L13":1095,"50S RIBOSOMAL PROTEIN L14":1095,"50S RIBOSOMAL PROTEIN L15":1095,"50S RIBOSOMAL PROTEIN L18":1095,"50S RIBOSOMAL PROTEIN L19":1095,"50S RIBOSOMAL PROTEIN L2":1095,"50S RIBOSOMAL PROTEIN L3":1095,"50S RIBOSOMAL PROTEIN L30":1095,"50S RIBOSOMAL PROTEIN L4":1095,"50S RIBOSOMAL PROTEIN L6":1095,"50S RIBOSOMAL PROTEIN L21":1093,"50S RIBOSOMAL PROTEIN L27":1093,"50S RIBOSOMAL PROTEIN L32":1093,"50S RIBOSOMAL PROTEIN L33":1093,"50S RIBOSOMAL PROTEIN L34":1093,"50S RIBOSOMAL PROTEIN L35":1093,"AMPA glutamate receptor activity":1092,"LIVER":1092,"glutathione metabolic process":1092,"protein import into nucleus":1092,"regulation of GTPase activity":1092,"DNA damage response, detection of DNA damage":1090,"core promoter binding":1090,"-!- The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP- ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.":1089,"ADP-ribosyltransferase (polymerizing). Poly(adenosine diphosphate ribose) polymerase. Poly(ADP-ribose) synthetase. Poly(ADP-ribose)polymerase.":1089,"NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D- ribosyl)(n+1)-acceptor.":1089,"NAD(+) ADP-ribosyltransferase.":1089,"endoplasmic reticulum exit site":1089,"SUGAR (SUCROSE)":1088,"drug:proton antiporter activity":1088,"nucleotide-excision repair, DNA damage recognition":1088,"Aldehyde reductase.":1087,"glutathione derivative biosynthetic process":1087,"Agrobacterium fabrum str. C58":1086,"LIPID BINDING PROTEIN":1085,"heart development":1084,"lipid metabolic process":1083,"secretory granule membrane":1083,"synaptic vesicle membrane":1083,"Listeria monocytogenes EGD-e":1082,"positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle":1081,"DNA-directed RNA polymerase II subunit RPB11":1079,"50S ribosomal protein L24e":1078,"condensed nuclear chromosome":1076,"Enterococcus faecalis V583":1075,"SH3 domain binding":1074,"Cancer, Proteasome, Bortezomib, Drug Resistance, Binding Analysis, HYDROLASE-HYDROLASE INHIBITOR complex":1073,"generation of precursor metabolites and energy":1073,"regulation of macroautophagy":1073,"positive regulation of epidermal growth factor receptor signaling pathway":1072,"asymmetric synapse":1071,"positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway":1070,"regulation of small GTPase mediated signal transduction":1070,"Transferring groups other than amino-acyl groups.":1066,"sister chromatid cohesion":1064,"SUGAR (2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE)":1059,"JAK-STAT cascade involved in growth hormone signaling pathway":1058,"regulation of cholesterol biosynthetic process":1057,"GTPase activator activity":1056,"cellular response to heat":1056,"AMPA glutamate receptor complex":1055,"positive regulation of CD8-positive, alpha-beta T cell proliferation":1055,"ubiquitin-dependent ERAD pathway":1054,"DNA synthesis involved in DNA repair":1053,"tertiary granule membrane":1052,"OXYGEN STORAGE/TRANSPORT":1050,"Trypanosoma brucei":1050,"actin filament polymerization":1050,"regulation of autophagy":1050,"Trypanosoma brucei brucei TREU927":1049,"trans-Golgi network membrane":1047,"positive regulation of protein ubiquitination":1045,"positive regulation of telomere capping":1045,"NORWAY RAT":1044,"actin monomer binding":1044,"blood coagulation, extrinsic pathway":1044,"protein tyrosine phosphatase activity":1044,"PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER":1043,"Trypanosoma cruzi":1042,"LAURYL DIMETHYLAMINE-N-OXIDE":1040,"cell-cell adherens junction":1040,"positive regulation of DNA repair":1040,"protein targeting to mitochondrion":1039,"BERYLLIUM TRIFLUORIDE ION":1038,"regulation of JNK cascade":1036,"Golgi medial cisterna":1035,"regulation of synaptic transmission, glutamatergic":1034,"actin filament bundle assembly":1032,"undecameric":1032,"central nervous system development":1031,"60S RIBOSOMAL PROTEIN L10":1030,"Aquifex":1030,"NAD+ binding":1029,"cellular defense response":1026,"transcription corepressor activity":1026,"60 kDa chaperonin":1024,"cytokine-mediated signaling pathway":1024,"lipid binding":1023,"brewer's yeast,lager beer yeast,yeast":1022,"negative regulation of ERK1 and ERK2 cascade":1022,"3D7":1021,"protein sumoylation":1021,"Escherichia coli K12":1020,"Klebsiella pneumoniae":1020,"MAP kinase kinase activity":1020,"34-meric":1019,"BLOOD CLOTTING":1019,"NAD(P)-binding Rossmann-like Domain":1019,"high-density lipoprotein particle remodeling":1017,"actin cytoskeleton reorganization":1015,"nucleotide-excision repair, DNA gap filling":1015,"epithelial cell differentiation":1014,"mouse-ear cress,thale-cress":1014,"50S RIBOSOMAL PROTEIN L31":1011,"-!- This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). -!- A number of histones can act as acceptor.":1009,"ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.":1009,"Histidine kinase.":1009,"Histidine protein kinase. HK1. Protein histidine kinase. Protein kinase. Protein kinase (histidine).":1009,"adaptive immune response":1009,"DNA-directed RNA polymerase subunit beta":1008,"Enterococcus faecalis":1007,"BICARBONATE ION":1004,"VIRAL PROTEIN/IMMUNE SYSTEM":1003,"positive regulation of tyrosine phosphorylation of STAT protein":1003,"Bacteroides thetaiotaomicron":1002,"Glutamate receptor 2":1001,"Synechocystis sp. PCC 6803 substr. Kazusa":1001,"50S RIBOSOMAL PROTEIN L28":1000,"endosomal transport":1000,"50S ribosomal protein L4P":999,"positive regulation of B cell proliferation":999,"50S ribosomal protein L32e":998,"positive regulation of CD8-positive, alpha-beta T cell activation":998,"transferase/transferase inhibitor":998,"PYRUVIC ACID":997,"cell aging":997,"Phosphoric diester hydrolases.":996,"positive regulation of protein oligomerization":995,"-!- The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate. -!- Formerly EC 1.5.1.4.":994,"5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH.":994,"50S RIBOSOMAL PROTEIN L36":994,"Dihydrofolate reductase.":994,"Tetrahydrofolate dehydrogenase.":994,"positive regulation of memory T cell activation":994,"protein oligomerization":994,"(S)-lactate + NAD(+) = pyruvate + NADH.":993,"-!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme.":993,"L-lactate dehydrogenase.":993,"L-lactic acid dehydrogenase. L-lactic dehydrogenase.":993,"single organismal cell-cell adhesion":992,"respiratory chain complex IV":991,"-!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. -!- The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. -!- All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). -!- The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. -!- For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle. -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. -!- To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule.":988,"2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.":988,"AhpC. Alkyl hydroperoxide reductase C22. PRDX. Prx. Thioredoxin peroxidase. TrxPx. Tryparedoxin peroxidase. TXNPx.":988,"Peroxiredoxin.":988,"nucleotide-binding oligomerization domain containing signaling pathway":988,"protein methylation":988,"regulation of cell cycle":988,"50S ribosomal protein L1":987,"actin filament":987,"cell motility":987,"phosphatidylinositol 3-kinase signaling":987,"HYDROLASE-HYDROLASE INHIBITOR complex, Proteasome, Mutant, Inhibitor, Binding Analysis":986,"B2M":985,"Phosphotransferases with an alcohol group as acceptor.":985,"cytosolic small ribosomal subunit":985,"-!- UTP, GTP, CTP, ITP and dATP can also act as donors. -!- Also phosphorylates hydroxylamine and fluoride in the presence of CO(2).":984,"ATP + pyruvate = ADP + phosphoenolpyruvate.":984,"Phosphoenol transphosphorylase. Phosphoenolpyruvate kinase.":984,"Pyruvate kinase.":984,"Human immunodeficiency virus type 1":978,"regulation of gene expression":978,"DNA polymerase IV":977,"messenger RNA":975,"regulation of actin cytoskeleton organization":975,"29-meric":974,"cellular response to virus":974,"negative regulation of MAP kinase activity":969,"Archaeoglobus":968,"26-meric":967,"thale cress":966,"50S ribosomal protein L11P":965,"RNA-directed 5'-3' RNA polymerase activity":964,"positive regulation of erythrocyte differentiation":963,"protein autoubiquitination":963,"steroid hormone receptor activity":963,"3'-UTR-mediated mRNA stabilization":962,"Danio rerio":962,"chromatin organization":962,"positive regulation of interleukin-8 production":961,"ubiquitin-dependent protein catabolic process":961,"negative regulation of smooth muscle cell proliferation":960,"response to cytokine":960,"DINUCLEAR COPPER ION":958,"viral transcription":958,"50S ribosomal protein L19E":955,"50S ribosomal protein L24E":955,"50S ribosomal protein L32E":955,"HLA-A, HLAA":955,"RNA polymerase II transcription factor complex":955,"50S ribosomal protein L4E":954,"PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER":953,"cellular response to interferon-gamma":953,"endothelial cell migration":953,"pig":952,"glycogen biosynthetic process":948,"telomere maintenance":948,"HEME-A":947,"ALPHA-D-MANNOSE":946,"protein serine/threonine/tyrosine kinase activity":946,"33-meric":945,"cellular protein modification process":945,"hydrolase/hydrolase inhibitor":944,"regulation of transcription involved in G1/S transition of mitotic cell cycle":944,"superoxide dismutase activity":944,"transcription from RNA polymerase I promoter":944,"Succinate + a quinone = fumarate + a quinol.":942,"BETA-D-MANNOSE":940,"THIOCYANATE ION":938,"Agrobacterium tumefaciens":937,"Protease":936,"endoplasmic reticulum-Golgi intermediate compartment":936,"lipid particle":936,"Methanothermobacter thermautotrophicus":935,"SUGAR (BETA-D-GLUCOSE)":935,"interstrand cross-link repair":935,"negative regulation of protein phosphorylation":935,"ribosome":935,"Transthyretin":934,"4 iron, 4 sulfur cluster binding":932,"Equus caballus":930,"negative regulation of anoikis":930,"regulation of gene silencing by miRNA":929,"peptidyl-prolyl cis-trans isomerase activity":928,"positive regulation of DNA binding":928,"protein destabilization":928,"2 iron, 2 sulfur cluster binding":927,"MSB8":927,"Sinorhizobium meliloti 1021":927,"activating transcription factor binding":926,"Arabidopsis":925,"chemoattractant activity":925,"DE NOVO PROTEIN":920,"MOUSE":920,"activation of protein kinase B activity":918,"Salmonella enterica subsp. enterica serovar Typhimurium":916,"G2 DNA damage checkpoint":915,"negative regulation of macrophage derived foam cell differentiation":915,"ruffle":915,"transcription from RNA polymerase III promoter":915,"hemolysis by symbiont of host erythrocytes":913,"lysine-acetylated histone binding":913,"-!- Ricin A-chain and related toxins show this activity. -!- Naked rRNA is attacked more slowly than rRNA in intact ribosomes. -!- Naked rRNA from Escherichia coli is cleaved at a corresponding position.":910,"Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.":910,"rRNA N-glycosidase.":910,"rRNA N-glycosylase.":910,"Nitric oxide synthase, endothelial":909,"positive regulation of guanylate cyclase activity":908,"positive regulation of viral genome replication":908,"maintenance of mitochondrion location":907,"protein localization":907,"sodium-independent organic anion transport":907,"-!- Acts on RNA-DNA hybrids.":905,"DNA-directed RNA polymerase I complex":905,"Endoribonuclease H. RNase H.":905,"Ribonuclease H.":905,"negative regulation of leukocyte cell-cell adhesion":905,"substrate adhesion-dependent cell spreading":905,"positive regulation of nitric-oxide synthase activity":904,"Endo-1,4-beta-xylanase.":902,"Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.":902,"cellular response to laminar fluid shear stress":902,"positive regulation of T cell proliferation":900,"BENZAMIDINE":898,"Cytochrome c oxidase subunit 2":898,"regulation of protein ubiquitination":897,"termination of RNA polymerase II transcription":897,"insulin receptor signaling pathway":893,"positive regulation of protein export from nucleus":893,"RNA polymerase I activity":892,"Neisseria meningitidis MC58":891,"mRNA export from nucleus":891,"Schizosaccharomyces pombe":890,"guanyl-nucleotide exchange factor activity":890,"Geobacillus kaustophilus HTA426":889,"VPI-5482":888,"60S RIBOSOMAL PROTEIN L13-A":887,"transcription factor complex":887,"mitotic cytokinesis":886,"50S ribosomal protein L10E":885,"60S RIBOSOMAL PROTEIN L11-B":885,"60S RIBOSOMAL PROTEIN L14-A":885,"BACTERIOCHLOROPHYLL A":884,"anthrax,anthrax bacterium":884,"50S RIBOSOMAL PROTEIN L1":883,"proteasome assembly":882,"DNA-directed RNA polymerase subunit alpha":881,"endocytosis":881,"G-protein coupled receptor binding":880,"Staphylococcus aureus subsp. aureus NCTC 8325":880,"Thermoplasma acidophilum DSM 1728":879,"brain development":879,"positive regulation of fibroblast proliferation":879,"spermatogenesis":878,"TRYPTOPHAN":876,"estrogen receptor binding":876,"positive regulation of cell cycle":876,"ubiquitin-specific protease binding":876,"calcium ion transport":875,"intracellular sequestering of iron ion":875,"skeletal system development":875,"catalase activity":871,"defense response":870,"positive regulation of RNA polymerase II transcriptional preinitiation complex assembly":869,"positive regulation of cell cycle arrest":869,"2,3-DIHYDROXY-1,4-DITHIOBUTANE":867,"ATP-binding cassette (ABC) transporter complex":862,"SUGAR (DECYL-BETA-D-MALTOPYRANOSIDE)":862,"Clostridium":861,"mRNA 3'-UTR binding":861,"centriole":860,"cholesterol biosynthetic process":860,"IMMUNOGLOBULIN":859,"site of double-strand break":859,"35-meric":857,"CONTRACTILE PROTEIN":857,"BRAIN":854,"CHOLIC ACID":854,"DNA-directed RNA polymerase subunit beta'":852,"Plasmodium":850,"positive regulation of vascular endothelial growth factor production":850,"Leishmania major":849,"positive regulation of translation":849,"STRUCTURAL PROTEIN/DNA":847,"regulation of mitochondrial membrane potential":847,"positive regulation of proteolysis":845,"ficolin-1-rich granule membrane":844,"intracellular estrogen receptor signaling pathway":844,"positive regulation of mitotic cell cycle":843,"22-meric":842,"histone demethylase activity":842,"response to toxic substance":842,"(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE":841,"protein localization to chromatin":841,"BACILLUS SUBTILIS":840,"cyclooxygenase pathway":840,"Dihydrofolate reductase":839,"regulation of necroptotic process":839,"response to retinoic acid":839,"ATPase activity, coupled":838,"In linear amides.":838,"African clawed frog":837,"Burkholderia pseudomallei 1710b":837,"5S Ribosomal RNA":836,"negative regulation of ERBB signaling pathway":836,"pericentriolar material":836,"Azotobacter vinelandii":835,"cell redox homeostasis":835,"positive regulation of catalytic activity":835,"regulation of type I interferon production":835,"GTPase binding":834,"23S Ribosomal RNA":833,"Chlamydomonas reinhardtii":833,"cytoplasmic viral factory":833,"transcription elongation from RNA polymerase III promoter":833,"protein processing":832,"ruffle membrane":831,"structural molecule activity":831,"histone-lysine N-methyltransferase activity":830,"leukocyte cell-cell adhesion":830,"zymogen binding":830,"Virus":829,"16S RIBOSOMAL RNA":828,"ETHANOL":828,"positive regulation of cell adhesion":826,"DNA-directed RNA polymerase III complex":825,"hydrolase activity":825,"Pseudomonas fluorescens":824,"positive regulation of NIK/NF-kappaB signaling":824,"response to tumor necrosis factor":824,"Aeropyrum pernix K1":823,"catalytic domain":823,"50S ribosomal protein L10":822,"SEE REMARK 999":820,"negative regulation of DNA damage response, signal transduction by p53 class mediator":820,"Haemophilus":818,"negative regulation of cell death":818,"regulation of type I interferon-mediated signaling pathway":818,"Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds.":817,"Hepatitis C virus":816,"epithelial to mesenchymal transition":816,"2-OXOGLUTARIC ACID":815,"Bacillus cereus ATCC 14579":815,"glutathione peroxidase activity":815,"VF5":814,"positive regulation of intrinsic apoptotic signaling pathway":814,"vesicle-mediated transport":813,"Bacterioferritin":812,"Exoribonucleases producing 5'-phosphomonoesters.":812,"chaperone-mediated protein folding":812,"regulation of cell migration":812,"50S RIBOSOMAL PROTEIN L10E":811,"positive regulation of telomere maintenance via telomerase":811,"-!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).":810,"CYTOKINE":810,"Protein phosphatase-1. Protein phosphatase-2A. Protein phosphatase-2B. Protein phosphatase-2C. Serine/threonine specific protein phosphatase.":810,"Protein-serine/threonine phosphatase.":810,"[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.":810,"bacterial-type RNA polymerase transcriptional repressor activity, sequence-specific DNA binding":810,"maltodextrin transport":810,"BOS TAURUS":809,"((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.":806,"-!- This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. -!- Some of these enzymes catalyze the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. -!- The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. -!- The description (accepted name) of the enzyme should be modified for each specific instance by substituting 'glycogen' with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.":806,"Amylophosphorylase. Muscle phosphorylase a and b. Polyphosphorylase.":806,"Glycogen phosphorylase.":806,"fatty acid biosynthetic process":806,"Hydrolase/Hydrolase Inhibitor":805,"cell differentiation":805,"secretory granule":805,"Cytochrome c oxidase subunit 1":804,"Yeast":804,"estrogen response element binding":804,"fruit fly":803,"positive regulation of type I interferon production":803,"tRNA transcription from RNA polymerase III promoter":803,"BACTERIOPHEOPHYTIN A":802,"40S RIBOSOMAL PROTEIN S27-A":801,"40S RIBOSOMAL PROTEIN S28-A":801,"40S RIBOSOMAL PROTEIN S29-A":801,"40S RIBOSOMAL PROTEIN S30-A":801,"GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-LIKE PROTEIN":801,"PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER":801,"SUPPRESSOR PROTEIN STM1":801,"UBIQUITIN-40S RIBOSOMAL PROTEIN S31":801,"-!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.":800,"An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH.":800,"Enoyl-ACP reductase. NADH-enoyl acyl carrier protein reductase. NADH-specific enoyl-ACP reductase.":800,"Enoyl-[acyl-carrier-protein] reductase (NADH).":800,"Green fluorescent protein":800,"chloroplast stroma":800,"glucose metabolic process":800,"40S RIBOSOMAL PROTEIN S26-B":799,"Streptomyces coelicolor":799,"POL":798,"ligand-dependent nuclear receptor transcription coactivator activity":797,"Sus":796,"Thermococcus kodakarensis KOD1":795,"-!- A group of enzymes that oxidize primary monoamines but have little or no activity toward diamines, such as histamine, or toward secondary and tertiary amines. -!- They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. -!- In some mammalian tissues the enzyme also functions as a vascular- adhesion protein (VAP-1). -!- Formerly EC 1.4.3.6.":794,"Amine oxidase. Amine oxidase (copper-containing). Benzylamine oxidase. CAO. Copper amine oxidase.":794,"Primary-amine oxidase.":794,"RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2).":794,"negative regulation of cell cycle arrest":794,"protein deglycosylation":794,"antigen processing and presentation":793,"host cell cytoplasm":793,"16S Ribosomal RNA":792,"-!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors.":791,"ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.":791,"NDK. Nucleoside 5'-diphosphate phosphotransferase. Nucleoside diphosphokinase.":791,"Nucleoside-diphosphate kinase.":791,"SH3/SH2 adaptor activity":791,"SUGAR (MALTOSE)":791,"protein binding, bridging":791,"COPII vesicle coating":790,"-!- This enzyme also catalyzes the phosphorylation of PtdIns4P to PtdIns(3,4)P(2), and of PtdIns to PtdIns3P.":789,"ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.":789,"Laminin":789,"Phosphatidylinositol-4,5-bisphosphate 3-kinase.":789,"Type I phosphoinositide 3-kinase.":789,"endonuclease activity":789,"positive regulation of cyclase activity":789,"response to cadmium ion":789,"PLANT PROTEIN":788,"UNP residues 21-119":788,"canonical Wnt signaling pathway":788,"termination of RNA polymerase III transcription":788,"-!- Can introduce negative superhelical turns into double-stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.99.1.2).":787,"ATP-dependent breakage, passage and rejoining of double-stranded DNA.":787,"DNA gyrase. DNA topoisomerase II. Type II DNA topoisomerase.":787,"DNA topoisomerase (ATP-hydrolyzing).":787,"SARS coronavirus":787,"activation of phospholipase C activity":786,"neuromuscular junction":785,"Aspartic endopeptidases.":784,"maltose transport":784,"maltose transport complex":784,"host cell nucleus":783,"Z disc":782,"Zea mays":781,"positive regulation of mitotic nuclear division":781,"pyruvate metabolic process":780,"titin binding":780,"-!- From entero-, rhino-, aphto- and cardioviruses. -!- Larger than the homologous virus picornain 2A. -!- Belongs to peptidase family C3.":779,"-!- Similar enzymes: venom RNase, Thiobacillus thioparus RNase, Xenopus laevis RNase, Rhizopus oligosporus RNase, ribonuclease M. -!- Formerly EC 2.7.7.16 and EC 3.1.4.22.":779,"DNA damage induced protein phosphorylation":779,"Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.":779,"Foot-and-mouth protease 3C. Picornavirus endopeptidase 3C. Poliovirus protease 3C. Rhinovirus protease 3C.":779,"Pancreatic RNase. Ribonuclease I. RNase. RNase A. RNase I.":779,"Pancreatic ribonuclease.":779,"Picornain 3C.":779,"Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.":779,"50S RIBOSOMAL PROTEIN L10":777,"STREPTOCOCCUS PNEUMONIAE":777,"Trypanosoma cruzi strain CL Brener":777,"positive regulation of pathway-restricted SMAD protein phosphorylation":777,"(1) An alcohol + NAD(+) = an aldehyde or ketone + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.":776,"-!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.":776,"Alcohol dehydrogenase.":776,"cAMP binding":776,"Mitogen-activated protein kinase 14":774,"iron ion homeostasis":773,"spindle organization":773,"Mus musculus, Homo sapiens":772,"monocyte differentiation":772,"regulation of protein localization":772,"virus receptor activity":772,"Drosophila":771,"peroxisomal matrix":771,"Paracoccus denitrificans":770,"TIGR4":770,"filamentous actin":770,"phosphatase activity":770,"phosphatidylinositol-3,4,5-trisphosphate binding":770,"reactive oxygen species metabolic process":770,"transcriptionally active chromatin":770,"-!- The reaction is catalyzed by two types of enzymes, found in the perimplasm of denitrifying bacteria. -!- One type comprises proteins containing multiple copper centers, the other a heme protein, cytochrome cd1. -!- Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. -!- Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. -!- May also catalyze the reaction of EC 1.7.99.1 since this is a well- known activity of cytochrome cd1. -!- Formerly EC 1.6.6.5, EC 1.7.99.3 and EC 1.9.3.2.":769,"Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+).":769,"Nitrite reductase (NO-forming).":769,"cd-cytochrome nitrite reductase. Cytochrome c-551:O(2), NO(2)(+) oxidoreductase. Cytochrome cd. Cytochrome cd1. Hydroxylamine (acceptor) reductase. Methyl viologen-nitrite reductase. Nitrite reductase. Nitrite reductase (cytochrome). Nitrite reductase (cytochrome; NO-forming). Pseudomonas cytochrome oxidase.":769,"negative regulation of autophagy":769,"regulation of peptidyl-tyrosine phosphorylation":769,"Aequorea victoria":768,"Dictyostelium discoideum":766,"Methanocaldococcus":766,"Trypanosoma":766,"3-dehydroquinate = 3-dehydroshikimate + H(2)O.":765,"3-dehydroquinate dehydratase.":765,"Burkholderia pseudomallei":765,"Sinorhizobium meliloti":765,"chaperone-mediated autophagy":765,"cysteine-type peptidase activity":765,"mitotic spindle organization":765,"regulation of cellular amino acid metabolic process":765,"AMMONIUM ION":764,"COPPER (I) ION":764,"calcium-mediated signaling":762,"5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.":761,"60-meric":761,"Thymidylate synthase.":761,"mitochondrial proton-transporting ATP synthase complex":761,"negative regulation of cell migration":761,"nuclear chromosome":761,"Cytochrome b":760,"GroEL-GroES complex":760,"receptor clustering":760,"Aspartate carbamoyltransferase.":759,"Aspartate transcarbamylase. ATCase. Carbamylaspartotranskinase.":759,"Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.":759,"tricarboxylic acid cycle":759,"Histone-lysine N-methyltransferase.":758,"Protein methylase 3. Protein methylase III. Protein methyltransferase II. Protein-lysine N-methyltransferase.":758,"S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].":758,"regulation of cytokine production involved in inflammatory response":758,"sarcoplasmic reticulum":758,"TBP-class protein binding":757,"cholesterol homeostasis":757,"defense response to fungus":757,"lipopolysaccharide-mediated signaling pathway":757,"-!- Belongs to peptidase family S14.":756,"Caseinolytic protease. Endopeptidase Ti. Protease Ti.":756,"Endopeptidase Clp.":756,"Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).":756,"MOTOR PROTEIN":756,"DNA damage checkpoint":755,"ARGININE":754,"UBIQUINONE-10":753,"positive regulation of exocytosis":753,"negative regulation of extrinsic apoptotic signaling pathway in absence of ligand":752,"regulation of DNA repair":752,"glycosphingolipid metabolic process":750,"T cell differentiation in thymus":749,"prostaglandin biosynthetic process":749,"endoplasmic reticulum-Golgi intermediate compartment membrane":748,"extrinsic apoptotic signaling pathway in absence of ligand":748,"positive regulation of production of miRNAs involved in gene silencing by miRNA":748,"2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL":747,"HORMONE":747,"protein polymerization":747,"positive regulation of nitric-oxide synthase biosynthetic process":746,"transport vesicle membrane":745,"Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819":744,"TETRAFLUOROALUMINATE ION":744,"-!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. -!- Thiols can replace phosphate.":743,"Corynebacterium glutamicum ATCC 13032":743,"D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.":743,"GAPDH. NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase.":743,"Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).":743,"MYRISTIC ACID":743,"Vibrio":743,"2'-DEOXYADENOSINE 5'-TRIPHOSPHATE":742,"phosphoprotein phosphatase activity":742,"autophagosome maturation":741,"Nos1, Bnos":739,"Thermoplasma acidophilum":739,"endoribonuclease activity":739,"ACETYL COENZYME *A":738,"chromosome segregation":737,"PALMITIC ACID":736,"Spinacia oleracea":736,"recycling endosome":736,"-!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements.":735,"-!- Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. -!- Formerly EC 1.1.1.70.":735,"ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine.":735,"Aldehyde dehydrogenase (NAD(+)).":735,"An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH.":735,"Glutamate--ammonia ligase. L-glutamine synthetase.":735,"Glutamine synthetase.":735,"cellular response to calcium ion":735,"polyubiquitin binding":734,"Toxoplasma gondii":733,"transporter activity":732,"-!- Encoded by the genome of the viruses of the hepatitis C group, and contributes to the maturation of the precursor polyproteins. -!- The enzyme is greatly activated by binding of the 54-residue NS4A 'cofactor' protein also derived from the viral polyprotein. -!- Belongs to peptidase family S29.":731,"43":731,"Cpro-2. Hepatitis C virus NS3 serine proteinase.":731,"Hepacivirin.":731,"Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.":731,"LYASE/LYASE INHIBITOR":728,"negative regulation of neuron apoptotic process":728,"MFS general substrate transporter like domains":727,"Mycobacterium smegmatis":727,"REPLICATION":727,"hemoglobin binding":725,"positive regulation of interleukin-12 secretion":725,"troponin I binding":725,"-!- SARS coronavirus main protease is the key enzyme in SARS coronavirus replicase polyprotein processing. -!- Belongs to peptidase family C30.":724,"3C-like protease. 3cLpro. Coronavirus 3C-like protease. SARS coronavirus main protease. SARS-CoV 3CLpro enzyme. Severe acute respiratory syndrome coronavirus main protease.":724,"SARS coronavirus main proteinase.":724,"TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.":724,"cellular response to transforming growth factor beta stimulus":723,"integrin complex":723,"DNA-directed RNA polymerase subunit omega":722,"cell growth":722,"positive regulation of protein targeting to mitochondrion":722,"in utero embryonic development":721,"Dipeptidyl peptidase 4":720,"Metalloendopeptidases.":720,"Transaminases.":720,"Ribosome/Antibiotic":719,"chaperone-mediated protein complex assembly":719,"chromatin":719,"antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent":718,"negative regulation of telomere maintenance via telomere lengthening":718,"protein localization to chromosome, telomeric region":718,"nucleosome assembly":716,"Fab":715,"Actin, alpha skeletal muscle":714,"-!- A membrane-bound serine-type peptidase in mammals. -!- EC 3.4.14.11 catalyzes a similar reaction. -!- Belongs to peptidase family S9B.":713,"-!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.":713,"Acting on ATP; involved in cellular and subcellular movement.":713,"D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate.":713,"Dipeptidyl aminopeptidase IV. DPP IV. Gly-Pro naphthylamidase. Post-proline dipeptidyl aminopeptidase IV. Xaa-Pro-dipeptidylaminopeptidase.":713,"Dipeptidyl-peptidase IV.":713,"Fructose 1,6-bisphosphatase. Hexose diphosphatase.":713,"Fructose-bisphosphatase.":713,"Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.":713,"THERMUS THERMOPHILUS":713,"glucose transport":713,"hyperosmotic response":713,"positive regulation of protein serine/threonine kinase activity":712,"coreceptor activity":711,"nuclear outer membrane-endoplasmic reticulum membrane network":711,"transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding":710,"estrogen receptor activity":708,"kinetochore":708,"positive regulation of cytosolic calcium ion concentration":708,"regulation of cell adhesion":708,"bioluminescence":707,"Glycine max":706,"Ribonuclease pancreatic":706,"bovine":706,"positive regulation of protein tyrosine kinase activity":706,"virion attachment to host cell":706,"Acinetobacter baumannii":705,"B2m":705,"50S RIBOSOMAL PROTEIN L11":704,"intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator":704,"negative regulation of protein ubiquitination":704,"50S RIBOSOMAL PROTEIN L11P":703,"ACIDIC RIBOSOMAL PROTEIN P0 HOMOLOG":703,"tropomyosin binding":702,"Aplysia californica":701,"chromosome":701,"Gloeobacter violaceus PCC 7421":700,"HYDROLASE INHIBITOR":700,"bicellular tight junction":700,"cell outer membrane":700,"extrinsic apoptotic signaling pathway":700,"-!- The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. -!- It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). -!- In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. -!- Cf. EC 1.3.5.4.":699,"Succinate dehydrogenase (quinone).":699,"Succinate dehydrogenase (ubiquinone). Succinic dehydrogenase.":699,"TFIIB-class transcription factor binding":699,"Ubiquitin":699,"fibrinogen complex":698,"insulin binding":698,"renal absorption":698,"transcriptional preinitiation complex":698,"Glutamine synthetase":697,"MyD88-independent toll-like receptor signaling pathway":697,"PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER":697,"late endosome membrane":696,"positive regulation of focal adhesion assembly":695,"RNA polymerase II transcription factor activity, estrogen-activated sequence-specific DNA binding":694,"kidney development":694,"positive stranded viral RNA replication":694,"27-meric":693,"DNA recombination":693,"Tubulin alpha-1B chain":693,"positive regulation of neuron projection development":693,"RNA-directed RNA polymerase":692,"Zinc/RING finger domain, C3HC4 (zinc finger)":692,"macrophage differentiation":692,"mannose binding":692,"cytokine production":690,"positive regulation of protein kinase activity":690,"stress-induced premature senescence":689,"Neisseria meningitidis":688,"repressing transcription factor binding":688,"30S RIBOSOMAL PROTEIN S14 TYPE Z":687,"DNA polymerase binding":687,"lacZ":687,"ALPHA-L-FUCOSE":685,"Ribonuclease Inhibitor":684,"SMAD binding":684,"viral genome replication":684,"Bacillus halodurans C-125":683,"Clostridium botulinum":683,"amyloid fibril formation":683,"determination of adult lifespan":683,"(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE":682,"D-glyceraldehyde 3-phosphate = glycerone phosphate.":682,"Phosphotriose isomerase. Triose phosphoisomerase. Triosephosphate isomerase. Triosephosphate mutase.":682,"Triose-phosphate isomerase.":682,"myosin heavy chain binding":682,"-!- Composed of two proteins that can be separated but are both required for nitrogenase activity. -!- Dinitrogen reductase is a [4Fe-4S] protein, which, with two molecules of ATP and ferredoxin, generates an electron. -!- The electron is transferred to the other protein, dinitrogenase (molybdoferredoxin). -!- Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia; the molybdenum may be replaced by vanadium or iron. -!- The reduction is initiated by formation of hydrogen in stoichiometric amounts. -!- Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. -!- In the absence of a suitable substrate, hydrogen is slowly formed. -!- Ferredoxin may be replaced by flavodoxin (see EC 1.19.6.1). -!- Formerly EC 1.18.2.1.":681,"1,4-DIETHYLENE DIOXIDE":681,"8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 phosphate.":681,"Nitrogenase.":681,"Rhodobacter":681,"aerobic respiration":681,"2'-DEOXYURIDINE 5'-MONOPHOSPHATE":680,"Ovis aries":680,"laminin binding":680,"mitotic spindle assembly":680,"phagocytosis":680,"endosome lumen":678,"Rhodopseudomonas palustris CGA009":677,"anatomical structure morphogenesis":677,"Maltose-binding periplasmic protein":676,"BETA-D-GALACTOSE":675,"Rac GTPase binding":675,"T cell differentiation":675,"positive regulation of actin cytoskeleton reorganization":675,"regulation of early endosome to late endosome transport":675,"regulation of erythrocyte differentiation":675,"response to molecule of bacterial origin":675,"Epidermal growth factor receptor":674,"Streptococcus mutans UA159":673,"Sulfolobus tokodaii str. 7":673,"THYMIDINE-5'-TRIPHOSPHATE":673,"viral process":673,"branched-chain amino acid catabolic process":672,"ethanol oxidation":672,"P2":671,"Staphylococcus aureus subsp. aureus COL":671,"protein kinase C binding":671,"2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE":670,"CATALYTIC DOMAIN":670,"positive regulation of establishment of protein localization to plasma membrane":670,"(1) Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. (2) Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate.":669,"-!- Specificity not completely determined. -!- Can also catalyze ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5.":669,"Deinococcus radiodurans":669,"Inosine phosphorylase. PNPase.":669,"PEPTIDE BINDING PROTEIN":669,"Purine-nucleoside phosphorylase.":669,"epoxide hydrolase activity":669,"muscle contraction":669,"protein import into nucleus, translocation":669,"heterotypic cell-cell adhesion":667,"3-dehydroquinate dehydratase":666,"B cell differentiation":666,"regulation of cytoskeleton organization":666,"-!- The enzyme from higher eukaryotes is identical with EC 2.4.2.10.":665,"OMP decarboxylase. OMPdcase. Orotidine-5'-phosphate carboxy-lyase. Orotidylic decarboxylase. UMP synthase. Uridine 5'-monophosphate synthase.":665,"Orotidine 5'-phosphate = UMP + CO(2).":665,"Orotidine-5'-phosphate decarboxylase.":665,"cytoplasmic vesicle membrane":665,"antioxidant activity":664,"-!- A large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. -!- They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. -!- They include peroxin, which apparently is involved in Zellweger's syndrome.":663,"60S ACIDIC RIBOSOMAL PROTEIN P0":663,"GLYCINE":663,"Superoxide dismutase [Cu-Zn]":663,"Vesicle-fusing ATPase.":663,"activation of protein kinase activity":663,"cellular response to glucose starvation":662,"-!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. -!- This activity can be formed from EC 2.6.1.57 by controlled proteolysis.":661,"Aspartate aminotransferase. Glutamic--aspartic transaminase. Glutamic--oxaloacetic transaminase. Transaminase A.":661,"Aspartate transaminase.":661,"CYANIDE ION":661,"L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.":661,"Streptococcus pyogenes":661,"23S ribosomal rna":660,"DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER":660,"fatty acid beta-oxidation":660,"mitogen-activated protein kinase p38 binding":660,"peptidyl-diphthamide biosynthetic process from peptidyl-histidine":660,"protein auto-ADP-ribosylation":660,"CELL DIVISION PROTEIN KINASE 2":659,"histone deacetylase activity":659,"regulation of protein kinase activity":659,"retrograde vesicle-mediated transport, Golgi to ER":659,"cellular protein localization":658,"positive regulation of transcription elongation from RNA polymerase II promoter":658,"rRNA processing":658,"enzyme activator activity":657,"negative regulation of production of miRNAs involved in gene silencing by miRNA":657,"peroxisomal membrane":657,"positive regulation of phagocytosis":657,"Glutamic dehydrogenase.":656,"aldehyde dehydrogenase [NAD(P)+] activity":656,"Cytochrome c oxidase subunit 3":655,"Polyubiquitin-C":655,"tRNA binding":655,"catalytic step 2 spliceosome":654,"positive regulation of phospholipase activity":654,"response to endoplasmic reticulum stress":654,"(7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM 4-OXIDE":653,"DNA polymerase eta":653,"osteoblast differentiation":653,"-!- Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position.":652,"Cyclin-A2":652,"Lecithinase A. Phosphatidase. Phosphatidolipase. Phosphatidylcholine 2-acylhydrolase. Phospholipase A2.":652,"Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate.":652,"Phospholipase A(2).":652,"SULFOLOBUS SOLFATARICUS":652,"TRISTEAROYLGLYCEROL":652,"VCP-NPL4-UFD1 AAA ATPase complex":652,"LYSOZYME":651,"dipeptidyl-peptidase activity":651,"3',5'-cyclic-AMP phosphodiesterase activity":650,"Aeropyrum pernix":650,"regulation of double-strand break repair via homologous recombination":650,"CA2":649,"Stathmin-4":649,"actin filament bundle":649,"cellular protein complex assembly":648,"nuclear-transcribed mRNA catabolic process, nonsense-mediated decay":648,"cellular nitrogen compound metabolic process":647,"tRNA aminoacylation for protein translation":647,"-!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13.":646,"D-alanyl-D-alanine carboxypeptidase. DD-peptidase. DD-transpeptidase.":646,"Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.":646,"Serine-type D-Ala-D-Ala carboxypeptidase.":646,"phosphatidylcholine biosynthetic process":646,"positive regulation of cysteine-type endopeptidase activity involved in apoptotic process":646,"protein insertion into membrane":646,"mesoderm development":645,"protein N-linked glycosylation via asparagine":645,"response to UV-A":645,"BMP signaling pathway":643,"METHIONINE":643,"-!- Acts on N-acetylglucosides and N-acetylgalactosides. -!- Formerly EC 3.2.1.29 and EC 3.2.1.30.":642,"2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE":642,"Beta-N-acetylhexosaminidase.":642,"Beta-hexosaminidase. Hexosaminidase. N-acetyl-beta-glucosaminidase.":642,"Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.":642,"nucleotide-excision repair, DNA incision, 3'-to lesion":642,"nucleotide-excision repair, preincision complex stabilization":642,"primary amine oxidase activity":642,"Estrogen receptor":641,"intrinsic apoptotic signaling pathway":641,"regulation of endocytosis":641,"Carboxylic ester hydrolases.":640,"activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c":640,"phagocytic vesicle":640,"ATP synthesis coupled proton transport":639,"POLB":639,"Proton-gated ion channel":639,"peroxisome proliferator activated receptor signaling pathway":639,"transmembrane receptor protein tyrosine kinase signaling pathway":639,"beta-lactamase activity":638,"neuron apoptotic process":638,"positive regulation of superoxide anion generation":638,"rabbit":638,"response to salt stress":638,"dendritic cell chemotaxis":636,"50S RIBOSOMAL PROTEIN L9":635,"embryo implantation":635,"host cell cytosol":635,"negative regulation of tumor necrosis factor production":635,"phosphatidylinositol 3-kinase activity":635,"5S RRNA":634,"RNA polymerase II core binding":634,"-!- Also catalyzes transcarboxylation; the plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA.":633,"ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.":633,"Acetyl-CoA carboxylase.":633,"inner ear development":633,"SUGAR (ALPHA-D-GLUCOSE)":632,"negative regulation of angiogenesis":632,"2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE":631,"ATP metabolic process":631,"Listeria monocytogenes":631,"RNA polymerase II transcription factor activity, sequence-specific DNA binding":631,"linoleic acid metabolic process":631,"response to gamma radiation":631,"retrograde protein transport, ER to cytosol":631,"Ligase":630,"aldehyde dehydrogenase (NAD) activity":630,"negative regulation of neuron death":630,"negative regulation of viral genome replication":630,"telomere maintenance via telomerase":630,"50S Ribosomal Protein L15E":629,"50S ribosomal protein L7AE":629,"Derlin-1 retrotranslocation complex":629,"protein kinase B signaling":629,"B cell receptor signaling pathway":628,"Fission yeast":628,"NF-kappaB binding":628,"Tubulin beta chain":628,"-!- Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.":627,"7-methylguanosine mRNA capping":627,"Avicelase. Beta-1,4-endoglucan hydrolase. Beta-1,4-glucanase. Carboxymethyl cellulase. Celludextrinase. Endo-1,4-beta-D-glucanase. Endo-1,4-beta-D-glucanohydrolase. Endo-1,4-beta-glucanase. Endoglucanase.":627,"Cellulase.":627,"Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.":627,"Glycogen phosphorylase, muscle form":627,"Thermonuclease":627,"Transferase/Transferase Inhibitor":627,"establishment of protein localization to plasma membrane":627,"positive regulation of actin-dependent ATPase activity":627,"60S RIBOSOMAL PROTEIN L5":626,"cellular response to cAMP":626,"pol":625,"response to UV-C":625,"intrinsic apoptotic signaling pathway by p53 class mediator":624,"positive regulation of inflammatory response":624,"positive regulation of release of cytochrome c from mitochondria":624,"regulation of cholesterol metabolic process":624,"MHC class II protein complex":623,"positive regulation of JNK cascade":623,"Copper-containing nitrite reductase":622,"Protein biosynthesis, ribosomes, RNA, tRNA, transfer RNA, 30S, 70S, 16S, 23S, ribosomal subunit, RIBOSOME":622,"endoplasmic reticulum mannose trimming":622,"invadopodium membrane":622,"regulation of rhodopsin mediated signaling pathway":622,"steroid metabolic process":622,"positive regulation of peptidyl-threonine phosphorylation":621,"2-CARBOXYARABINITOL-1,5-DIPHOSPHATE":620,"ATP synthase subunit alpha, mitochondrial":620,"LUMINESCENT PROTEIN":620,"ER overload response":619,"Enterococcus":619,"Histone H3.2":619,"Oryza sativa Japonica Group":619,"endodermal cell differentiation":619,"transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding":619,"transition metal ion binding":619,"1021":618,"response to insulin":618,"Transitional endoplasmic reticulum ATPase":617,"ATP synthase subunit beta, mitochondrial":616,"negative regulation of nitric-oxide synthase biosynthetic process":616,"BETA-2-MICROGLOBULIN":615,"cobalt ion binding":615,"mRNA processing":615,"positive regulation of cytokine production":614,"positive regulation of heterotypic cell-cell adhesion":614,"2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O.":613,"Cytochrome-c peroxidase.":613,"RNA-protein complex, RIBOSOME":613,"Thermosynechococcus elongatus BP-1":613,"positive regulation of mitochondrial membrane potential":613,"Alcaligenes faecalis":612,"LBD domain binding":612,"SUGAR (8-MER)":611,"T cell chemotaxis":611,"carbohydrate transport":611,"regulation of mitotic cell cycle":611,"metallopeptidase activity":610,"negative regulation of fibroblast proliferation":610,"positive regulation of microtubule polymerization":610,"regulation of receptor activity":610,"translation initiation factor binding":610,"Shigella flexneri":609,"negative regulation of extracellular matrix disassembly":609,"ubiquitin-like protein ligase binding":609,"NAD metabolic process":608,"Thymidylate synthase":608,"DBD domain binding":607,"DNA biosynthetic process":607,"Paraburkholderia xenovorans LB400":607,"STAPHYLOCOCCUS AUREUS":607,"Synechococcus elongatus PCC 7942":607,"cardiac muscle contraction":607,"cellular response to actinomycin D":607,"cellular response to amino acid starvation":607,"positive regulation of JUN kinase activity":607,"response to organic substance":607,"steroid binding":607,"spliceosomal complex":606,"-!- A group of enzymes acetylating histones. -!- Several of the enzymes can also acetylate lysines in other proteins.":605,"Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine.":605,"Histone acetyltransferase.":605,"LECTIN":605,"Lysine acetyltransferase. Protein lysine acetyltransferase.":605,"N-terminal domain":605,"cellular response to interleukin-1":605,"cysteine-type endopeptidase inhibitor activity":605,"positive regulation of gene expression, epigenetic":605,"ribosome binding":605,"thiamine pyrophosphate binding":605,"cysteine-type endopeptidase activity involved in execution phase of apoptosis":604,"heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules":604,"histone acetyltransferase binding":604,"nuclear pore":604,"ATP-dependent Clp protease proteolytic subunit":603,"base-excision repair, gap-filling":603,"(3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase. Beta-hydroxyoctanoyl thioester dehydratase. Beta-hydroxyoctanoyl-ACP-dehydrase. Beta-hydroxyoctanoyl-acyl carrier protein dehydrase. D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase.":602,"-!- This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- The enzyme uses fatty acyl thioesters of ACP in vivo. -!- Different forms of the enzyme may have preferences for substrates with different chain length. -!- For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. -!- Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14. -!- Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0). -!- FabZ, but not FabA, can also accept unsaturated substrates. -!- Formerly EC 4.2.1.58, EC 4.2.1.60 and EC 4.2.1.61.":602,"3-hydroxyacyl-[acyl-carrier-protein] dehydratase.":602,"A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O.":602,"DNA-directed RNA polymerase II largest subunit":602,"leukotriene metabolic process":602,"DNA-BINDING PROTEIN":601,"RNA BINDING PROTEIN/RNA":601,"cellular response to organic cyclic compound":601,"sensory perception of sound":601,"(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH.":600,"-!- Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.":600,"-!- From entero- and rhinoviruses. -!- Smaller than the homologous virus picornain 3C. -!- Belongs to peptidase family C3.":600,"3-HYDROXY-3-CARBOXY-ADIPIC ACID":600,"3-oxoacyl-[acyl-carrier-protein] reductase.":600,"Picornain 2A.":600,"Picornavirus endopeptidase 2A. Poliovirus protease 2A. Rhinovirus protease 2A.":600,"Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.":600,"sarcoplasmic reticulum membrane":600,"bantam,chickens":599,"Cytochrome c peroxidase, mitochondrial":598,"HLA class II histocompatibility antigen, DR alpha chain":598,"peptidyl-tyrosine dephosphorylation":598,"response to superoxide":598,"Coagulation factor X":597,"DNA-directed RNA polymerase II 45 kDa polypeptide":597,"DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide":597,"DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide":597,"DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide":597,"Glyceraldehyde-3-phosphate dehydrogenase":597,"basal plasma membrane":597,"mitotic spindle pole":597,"protein binding involved in protein folding":597,"-!- A blood coagulation factor formed from the proenzyme factor X by limited proteolysis. -!- Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds. -!- The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca(2+) and phospholipids. -!- Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va. -!- Belongs to peptidase family S1.":596,"Coagulation factor Xa.":596,"DNA-directed RNA polymerase II 13.6 kDa polypeptide":596,"DNA-directed RNA polymerase II 140 kDa polypeptide":596,"DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide":596,"Prothrombase. Prothrombinase. Stuart factor. Thrombokinase.":596,"Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.":596,"iron ion transport":595,"mast cell degranulation":595,"negative chemotaxis":595,"Burkholderia thailandensis E264":594,"cell division":594,"cytochrome-c peroxidase activity":594,"DNA-directed RNA polymerase II subunit RPB7":593,"positive regulation of cardiac muscle cell proliferation":593,"NADP+ binding":592,"Replicase polyprotein 1ab":592,"positive regulation of G2/M transition of mitotic cell cycle":592,"positive regulation of positive chemotaxis":592,"cellular response to staurosporine":591,"negative regulation of telomerase activity":591,"IRE1-mediated unfolded protein response":590,"carbohydrate catabolic process":590,"response to osmotic stress":590,"filopodium":589,"intracellular protein transport":589,"neurotransmitter secretion":589,"nitric-oxide synthase regulator activity":589,"-!- Hydrolyzes double- or single-stranded substrate. -!- Similar enzymes: Chlamydomonas nuclease, spleen phosphodiesterase, spleen endonuclease. -!- Formerly EC 3.1.4.7.":588,"ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing":588,"Capsid protein VP1":588,"Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.":588,"Micrococcal endonuclease.":588,"Micrococcal nuclease.":588,"Streptococcus mutans":588,"T cell proliferation":588,"cytokinesis":588,"platelet alpha granule":588,"positive regulation of protein localization to plasma membrane":588,"protein disulfide isomerase activity":588,"SUCCINIC ACID":587,"clathrin-coated pit":587,"protein peptidyl-prolyl isomerization":587,"HORMONE/GROWTH FACTOR":586,"Staphylococcus aureus subsp. aureus N315":586,"hepatocyte growth factor receptor signaling pathway":586,"protein hexamerization":586,"cAMP-dependent protein kinase catalytic subunit alpha":585,"chromatin silencing at rDNA":585,"extrinsic component of membrane":585,"positive regulation of ATP biosynthetic process":585,"positive regulation of smooth muscle cell proliferation":585,"Schistosoma mansoni":584,"histone acetyltransferase complex":584,"-!- 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. -!- This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2.":583,"AP endonuclease class I. AP lyase. Deoxyribonuclease (apurinic or apyrimidinic). E.coli endonuclease III. Endodeoxyribonuclease (apurinic or apyrimidinic). Micrococcus luteus UV endonuclease. Phage-T(4) UV endonuclease. Phage-T4 UV endonuclease.":583,"Casein kinase II subunit alpha":583,"DNA-(apurinic or apyrimidinic site) lyase.":583,"OXALATE ION":583,"The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.":583,"VP1":583,"cellular senescence":583,"positive regulation of neuron apoptotic process":583,"ADENOSINE":582,"ARABIDOPSIS THALIANA":582,"Neuraminidase":582,"hippo signaling":582,"neuron migration":582,"regulation of cell-cell adhesion mediated by integrin":582,"spindle pole":582,"aldo-keto reductase (NADP) activity":581,"menaquinone biosynthetic process":581,"HYDROLASE-HYDROLASE INHIBITOR complex, Proteasome, Inhibitor, Binding Analysis":580,"HYDROLASE/RNA":580,"Rhodobacter sphaeroides 2.4.1":580,"cell-substrate adhesion":580,"-!- Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. -!- Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.":579,"3-ketoacyl-acyl carrier protein synthase. 3-oxoacyl-[acyl-carrier-protein] synthase. Acyl-malonyl acyl carrier protein-condensing enzyme. Acyl-malonyl(acyl-carrier-protein)-condensing enzyme. Beta-ketoacyl acyl carrier protein synthase. Beta-ketoacyl synthetase. Beta-ketoacyl-[acyl carrier protein] synthase. Beta-ketoacyl-ACP synthase I. Beta-ketoacyl-ACP synthetase. Beta-ketoacyl-acyl carrier protein synthetase. Beta-ketoacylsynthase. Condensing enzyme. Fatty acid condensing enzyme. KAS I.":579,"Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].":579,"Beta-ketoacyl-[acyl-carrier-protein] synthase I.":579,"DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator":579,"LIGASE/LIGASE INHIBITOR":579,"Legionella pneumophila subsp. pneumophila str. Philadelphia 1":579,"CYTIDINE-5'-TRIPHOSPHATE":577,"Integrase":577,"antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent":577,"hemopoiesis":577,"-!- Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. -!- Together with EC 1.6.2.4, it forms a system in which two reducing equivalents are supplied by NADPH. -!- Some of the reactions attributed to EC 1.14.15.3 belong here. -!- Formerly EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8 and EC 1.99.1.1.":576,"Aryl hydrocarbon hydroxylase. Aryl-4-monooxygenase. Cytochrome P450. Flavoprotein-linked monooxygenase. Microsomal monooxygenase. Microsomal P450. Xenobiotic monooxygenase.":576,"CHLOROPHYLL A":576,"ERK1 and ERK2 cascade":576,"Homeodomain-like":576,"RECEPTOR":576,"RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.":576,"Rhodobacter capsulatus":576,"Unspecific monooxygenase.":576,"cysteine-type endopeptidase activator activity involved in apoptotic process":576,"histone demethylase activity (H3-K9 specific)":576,"positive regulation of catenin import into nucleus":576,"angiotensin maturation":575,"epidermal growth factor-activated receptor activity":575,"HB27":574,"chloride ion binding":574,"detection of maltose stimulus":574,"maltose binding":574,"myelin sheath":574,"nematode":574,"regulation of mitotic nuclear division":574,"translational initiation":574,"Hemagglutinin HA1 chain":573,"S100 protein binding":573,"cellular response to iron(III) ion":573,"ferric iron import":573,"Entamoeba histolytica":572,"Streptomyces avidinii":572,"regulation of stress-activated MAPK cascade":572,"ribosomal protein S10":572,"ribosomal protein S11":572,"ribosomal protein S12":572,"ribosomal protein S13":572,"ribosomal protein S14":572,"ribosomal protein S15":572,"ribosomal protein S16":572,"ribosomal protein S17":572,"ribosomal protein S18":572,"ribosomal protein S19":572,"ribosomal protein S2":572,"ribosomal protein S20":572,"ribosomal protein S3":572,"ribosomal protein S4":572,"ribosomal protein S5":572,"ribosomal protein S6":572,"ribosomal protein S7":572,"ribosomal protein S8":572,"ribosomal protein S9":572,"ribosomal protein THX":572,"coenzyme binding":571,"decidualization":571,"fibroblast growth factor binding":571,"platelet-derived growth factor receptor binding":571,"positive regulation of transcription factor import into nucleus":571,"-!- The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo- chitodextrinases can act. -!- Activity is greatly stimulated in the presence of EC 1.14.99.53, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. -!- Cf. EC 3.2.1.202.":570,"-!- cAMP is required to activate this enzyme. -!- The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer composed of two regulatory (R) and two catalytic (C) subunits. -!- cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits (i.e. R(2)C(2) + 4 cAMP = R(2)(cAMP)(4) + 2 C). -!- Formerly EC 2.7.1.37.":570,"1,4-beta-poly-N-acetylglucosaminidase. Chitodextrinase. Poly-beta-glucosaminidase.":570,"26695":570,"ATP + biotin-[carboxyl-carrier-protein] + HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].":570,"Biotin carboxylase.":570,"Chitinase.":570,"PKA. PKA C. Protein kinase A.":570,"Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta- linkages in chitin and chitodextrins.":570,"cAMP-dependent protein kinase.":570,"chorismate biosynthetic process":570,"ribosomal small subunit binding":570,"BLOOD":568,"beta-catenin-TCF complex assembly":568,"microvillus":568,"regulation of establishment of endothelial barrier":568,"Streptavidin":567,"complement activation, alternative pathway":567,"positive regulation of interleukin-2 production":567,"positive regulation of protein kinase C activity":567,"regulation of mitotic centrosome separation":567,"Nostoc sp. PCC 7120":566,"CDK2":564,"Nucleoside diphosphate kinase":564,"cAMP-dependent protein kinase activity":564,"helicase activity":564,"viral entry into host cell":564,"Catalase HPII":563,"Streptococcus pneumoniae R6":563,"cellular response to epidermal growth factor stimulus":563,"positive regulation of substrate adhesion-dependent cell spreading":563,"wound healing":563,"Reverse transcriptase/ribonuclease H":562,"acetyltransferase activity":562,"molybdopterin cofactor binding":562,"negative regulation of cholesterol storage":562,"peptide catabolic process":562,"positive regulation of phosphatidylinositol 3-kinase activity":562,"transcriptional repressor complex":562,"Enoyl-[acyl-carrier-protein] reductase [NADH]":561,"negative regulation of thrombin-activated receptor signaling pathway":561,"platelet-derived growth factor receptor-beta signaling pathway":561,"Envelope glycoprotein gp160":560,"FE(8)-S(7) CLUSTER":560,"TPR domain binding":560,"peptidoglycan biosynthetic process":560,"positive regulation of cytokine secretion":560,"C-terminal domain":559,"Elongation factor G":559,"RNA splicing":559,"Vaccinia Virus protein VP39":559,"BAT3 complex binding":558,"D(-)-TARTARIC ACID":558,"Rhodopseudomonas palustris":558,"YVTN repeat-like/Quinoprotein amine dehydrogenase ":558,"histone H3 acetylation":558,"SERUM ALBUMIN":557,"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform":556,"regulation of protein catabolic process":556,"response to cold":556,"5'-deoxyribose-5-phosphate lyase activity":555,"Immunoglobulin heavy constant gamma 1":555,"cortical actin cytoskeleton organization":555,"protein tyrosine kinase binding":555,"With oxygen as acceptor.":554,"positive regulation of blood vessel endothelial cell migration":554,"postsynaptic membrane":554,"BACE1, BACE, KIAA1149":553,"DNA-directed RNA polymerase II subunit RPB4":553,"THERMOTOGA MARITIMA":553,"response to interleukin-1":553,"RNA polymerase II activating transcription factor binding":552,"Ribulose bisphosphate carboxylase large chain":552,"histone H4-K16 acetylation":552,"positive regulation of stress fiber assembly":552,"NONAETHYLENE GLYCOL":551,"positive regulation of actin filament polymerization":551,"GUANOSINE-5'-MONOPHOSPHATE":550,"cytoskeleton organization":550,"Orotidine 5'-phosphate decarboxylase":549,"Reaction center protein M chain":549,"positive regulation of interleukin-6 production":549,"response to cAMP":549,"Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)":548,"Reaction center protein L chain":548,"blood coagulation, fibrin clot formation":548,"calcium-dependent phospholipid binding":548,"MALONIC ACID":547,"activation of phospholipase A2 activity by calcium-mediated signaling":547,"microtubule organizing center":547,"multivesicular body, internal vesicle lumen":547,"negative regulation of cardiocyte differentiation":547,"Aspartate carbamoyltransferase regulatory chain":546,"cell projection":546,"chemokine activity":546,"36-meric":545,"Reaction center protein H chain":545,"snRNA transcription from RNA polymerase II promoter":545,"viral release from host cell":545,"3'-5'-exoribonuclease activity":544,"arginine binding":544,"cilium assembly":544,"mitotic cell cycle checkpoint":544,"translational elongation":544,",":543,"Ruminiclostridium thermocellum ATCC 27405":543,"interaction with symbiont":543,"negative regulation of interleukin-6 production":543,"positive regulation of apoptotic cell clearance":543,"3 iron, 4 sulfur cluster binding":542,"histone H3-K9 demethylation":542,"activation of MAPKK activity":541,"proteoglycan binding":541,"Francisella tularensis subsp. tularensis SCHU S4":540,"neuron differentiation":540,"retinoid X receptor binding":540,"18S RRNA":539,"DNA metabolic process":539,"Endoribonucleases producing other than 5'-phosphomonoesters.":539,"cell periphery":539,"negative regulation of cardiac muscle contraction":539,"2 acetyl-CoA = CoA + acetoacetyl-CoA.":538,"Acetoacetyl-CoA thiolase.":538,"Acetyl-CoA C-acetyltransferase.":538,"Lysozyme":538,"cell maturation":538,"regulation of cell cycle G2/M phase transition":538,"2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL":537,"HYDROLASE (O-GLYCOSYL)":537,"positive regulation of ubiquitin-protein transferase activity":537,"regulation of proteasomal protein catabolic process":537,"BACTEROIDES THETAIOTAOMICRON":536,"PLASMA":536,"Proto-oncogene tyrosine-protein kinase Src":536,"liver regeneration":536,"Ribonucleotide reductase.":535,"Serratia marcescens":535,"240-MERIC":534,"Acid--amino-acid ligases (peptide synthases).":534,"mitotic spindle":534,"MEMBRANE PROTEIN, TRANSPORT PROTEIN":533,"NADPH-hemoprotein reductase activity":532,"positive chemotaxis":532,"alpha-actinin binding":531,"cellular response to retinoic acid":531,"mitochondrial nucleoid":531,"neutrophil extravasation":531,"BETA-CAROTENE":530,"cell adhesion mediated by integrin":530,"negative regulation of gene expression, epigenetic":530,"negative regulation of inflammatory response":530,"positive regulation of pri-miRNA transcription from RNA polymerase II promoter":530,"-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. -!- The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.":529,"-!- Adds an N(7)-methylguanine cap to mRNA. -!- The nucleoside next to the terminal guanosine may be either guanosine or adenosine.":529,"Alpha-amylase.":529,"Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.":529,"Glycogenase.":529,"Guanine-7-methyltransferase. Messenger ribonucleate guanine 7-methyltransferase. Messenger RNA guanine 7-methyltransferase.":529,"NADH metabolic process":529,"Rho guanyl-nucleotide exchange factor activity":529,"S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.":529,"intrinsic component of plasma membrane":529,"mRNA (guanine-N(7)-)-methyltransferase.":529,"cortical actin cytoskeleton":528,"positive regulation of defense response to virus by host":528,"Cytochrome c oxidase subunit 4 isoform 1":527,"ER-associated misfolded protein catabolic process":527,"alphav-beta3 integrin-IGF-1-IGF1R complex":527,"regulation of interferon-gamma-mediated signaling pathway":527,"Histone H2A":526,"Methanothermobacter":526,"RETINAL":526,"Tankyrase-2":526,"fatty acid metabolic process":526,"mitochondrial transport":526,"natural killer cell chemotaxis":526,"phosphatidylinositol 3-kinase complex, class IB":526,"regulation of protein phosphorylation":526,"respiratory burst involved in defense response":526,"(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.":525,"-!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74).":525,"Enoyl hydrase. Unsaturated acyl-CoA hydratase.":525,"Enoyl-CoA hydratase.":525,"synaptic vesicle":525,"IGHG1":524,"-!- This enzyme catalyzes the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P450 monooxygenases (e.g. EC 1.14.14.1) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. -!- It also reduces cytochrome b5 and cytochrome c. -!- The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.":522,"Aldehyde reductase (NADPH-dependent). CPR. Cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent). Cytochrome P450 reductase. Dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase. FAD-cytochrome c reductase. Ferrihemoprotein P-450 reductase. NADP--cytochrome c reductase. NADP--cytochrome reductase. NADPH--cytochrome c oxidoreductase. NADPH--cytochrome c reductase. NADPH--cytochrome P450 oxidoreductase. NADPH--cytochrome P450 reductase. NADPH--ferricytochrome c oxidoreductase. NADPH--ferrihemoprotein reductase. NADPH-dependent cytochrome c reductase. NADPH:ferrihemoprotein oxidoreductase. NADPH:P450 reductase. Reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase. Reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate). TPNH(2) cytochrome c reductase. TPNH-cytochrome c reductase.":522,"DROSOPHILA MELANOGASTER":522,"Geobacillus kaustophilus":522,"NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein.":522,"NADPH--hemoprotein reductase.":522,"positive regulation of osteoblast differentiation":522,"ERAD pathway":521,"LYSINE":520,"NITRIC OXIDE":520,"NITRIC OXIDE SYNTHASE, BRAIN":520,"histone acetyltransferase activity":520,"keratinocyte differentiation":520,"-!- The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. -!- The mammalian enzyme also accepts 2'-deoxyuridine. -!- Formerly EC 2.4.2.23.":519,"AMP binding":519,"Acetylcholinesterase":519,"Pyrimidine phosphorylase. UPase. UrdPase.":519,"Structural Genomics, Unknown Function":519,"T-cell receptor alpha chain C region":519,"Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate.":519,"Uridine phosphorylase.":519,"positive regulation of Wnt signaling pathway":519,"30S Ribosomal Protein S10":518,"30S Ribosomal Protein S11":518,"30S Ribosomal Protein S12":518,"30S Ribosomal Protein S13":518,"30S Ribosomal Protein S14":518,"30S Ribosomal Protein S15":518,"30S Ribosomal Protein S16":518,"30S Ribosomal Protein S17":518,"30S Ribosomal Protein S18":518,"30S Ribosomal Protein S19":518,"30S Ribosomal Protein S2":518,"30S Ribosomal Protein S20":518,"30S Ribosomal Protein S3":518,"30S Ribosomal Protein S4":518,"30S Ribosomal Protein S5":518,"30S Ribosomal Protein S6":518,"30S Ribosomal Protein S7":518,"30S Ribosomal Protein S8":518,"30S Ribosomal Protein S9":518,"Aldehyde dehydrogenase":518,"Corynebacterium glutamicum":518,"Periplasmic binding protein-like II":518,"Rab GTPase binding":518,"macrophage derived foam cell differentiation":518,"telomerase holoenzyme complex assembly":518,"Bacillus sp.":517,"Hemagglutinin HA2 chain":517,"lipid biosynthetic process":517,"Aminopeptidases.":516,"Bacillus megaterium":516,"Hydrolases.":516,"cytoplasmic side of plasma membrane":516,"-!- Wide specificity for beta-D-glucosides. -!- Some examples also hydrolyze one or more of the following: beta-D- galactosides, alpha-L-arabinosides, beta-D-xylosides and beta-D- fucosides.":515,"60S RIBOSOMAL PROTEIN L3":515,"Agrobacterium":515,"Amygdalase. Beta-D-glucoside glucohydrolase. Cellobiase. Gentobiase.":515,"Beta-glucosidase.":515,"Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.":515,"phosphatase binding":515,"Kluyveromyces lactis NRRL Y-1140":514,"Shewanella oneidensis MR-1":514,"growth factor binding":514,"structural constituent of muscle":514,"XENON":513,"doxorubicin metabolic process":513,"N16961":512,"PHENYLALANINE":512,"Xanthomonas campestris pv. campestris str. ATCC 33913":512,"deubiquitinase activator activity":512,"folic acid binding":512,"Immune System":511,"Isomerase":511,"removal of superoxide radicals":511,"-!- Acts on a variety of acetic esters. -!- Also catalyzes transacetylations.":510,"Acetylcholine + H(2)O = choline + acetate.":510,"Acetylcholinesterase.":510,"Choline esterase I. Cholinesterase. True cholinesterase.":510,"androgen receptor binding":510,"purine nucleotide biosynthetic process":510,"-!- This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. -!- There are three types of this enzyme differing in their cofactors. -!- Class Ia enzymes contain a diferric-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. -!- In all cases the cofactors are involved in generation of a transient thiyl radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6 and EC 1.17.4.2.":509,"2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.":509,"RNA export from nucleus":509,"Ribonucleoside-diphosphate reductase.":509,"alcohol metabolic process":509,"virion":509,"Pyruvate kinase PKM":508,"Ribosome":508,"SUGAR (O-SIALIC ACID)":508,"anaerobic respiration":508,"flavin adenine dinucleotide catabolic process":508,"positive regulation of Lys63-specific deubiquitinase activity":508,"positive regulation of oxidative phosphorylation":508,"positive regulation of protein K63-linked deubiquitination":508,"regulation of aerobic respiration":508,"Cellular tumor antigen p53":507,"ubiquitin ligase complex":506,"23S RRNA":505,"Acriflavine resistance protein B":505,"Aldehyde dehydrogenase, mitochondrial":505,"SUGAR (BETA-D-MANNOSE)":505,"Uridine phosphorylase":505,"molybdenum ion binding":505,"negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator":505,"p51 RT":505,"-!- Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism. -!- It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides. -!- The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76. -!- Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate. -!- The enzyme can also use leukotriene A(4), the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B(4) as the product. -!- Formerly EC 3.3.2.3, EC 4.2.1.63 and EC 4.2.1.64.":504,"An epoxide + H(2)O = a glycol.":504,"Arene-oxide hydratase. Aryl epoxide hydrase. Cytosolic epoxide hydrolase. Epoxide hydrase. Epoxide hydratase. Trans-stilbene oxide hydrolase.":504,"COBALAMIN":504,"HYDROLASE/INHIBITOR":504,"Soluble epoxide hydrolase.":504,"replication fork":504,"-!- Activated by tubulin. -!- Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease. -!- Formerly EC 2.7.1.135.":503,"ATP + [tau protein] = ADP + [tau protein] phosphate.":503,"Sulfolobus tokodaii":503,"[Tau protein] kinase.":503,"[Tau-protein] kinase. Glycogen synthase kinase-3-beta. GSK. Protein tau kinase. Tau kinase. Tau-tubulin kinase. TPK. TTK.":503,"Complement C3":502,"Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821":502,"cellular response to dopamine":502,"daunorubicin metabolic process":502,"Canis lupus familiaris":501,"growth hormone receptor signaling pathway":501,"negative regulation of signal transduction":501,"neuron development":501,"-!- Is not activated by heavy metal ions. -!- Belongs to peptidase family M1. -!- Formerly EC 3.4.1.2, EC 3.4.3.5 and EC 3.4.13.6.":500,"Amino-oligopeptidase. Aminopeptidase M. Aminopeptidase N. Membrane alanine aminopeptidase. Membrane aminopeptidase I. Microsomal aminopeptidase. Particle-bound aminopeptidase. Peptidase E.":500,"Hydrolyzing N-glycosyl compounds.":500,"Membrane alanyl aminopeptidase.":500,"Oxidizing metal ions.":500,"Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.":500,"hippocampus development":500,"mitotic spindle assembly checkpoint":500,"negative regulation of intrinsic apoptotic signaling pathway":500,"proteolysis in other organism":500,"Gloeobacter violaceus":499,"exocytosis":499,"nucleobase-containing compound metabolic process":499,"-!- The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. -!- It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. -!- The mammalian enzyme contains cytochromes b-562, b-566 and C(1), and a 2-iron ferredoxin. -!- Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non- cytoplasmic compartment (cf. EC 1.6.99.3).":498,"Complex III (mitochondrial electron transport). Cytochrome bc1 complex. Ubiquinol--cytochrome-c reductase. Ubiquinone--cytochrome-c oxidoreductase.":498,"Golgi organization":498,"Quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H(+).":498,"Quinol--cytochrome-c reductase.":498,"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)":498,"response to light stimulus":498,"telomere capping":498,"DNA polymerase III subunit beta":497,"Heat shock cognate 71 kDa protein":497,"cysteine-type endopeptidase inhibitor activity involved in apoptotic process":497,"histone H4-K5 acetylation":497,"histone H4-K8 acetylation":497,"positive regulation of sprouting angiogenesis":497,"response to glucose":497,"-!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9.":496,"2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.":496,"60S RIBOSOMAL PROTEIN L4-A":496,"60S RIBOSOMAL PROTEIN L6-A":496,"60S RIBOSOMAL PROTEIN L7-A":496,"60S RIBOSOMAL PROTEIN L8-A":496,"60S RIBOSOMAL PROTEIN L9-A":496,"Carbamoyl phosphate synthetase. Carbamoyl-phosphate synthetase (glutamine-hydrolyzing). Carbamoylphosphate synthetase II. Carbamyl phosphate synthetase (glutamine). CPS. GD-CPSase. Glutamine-dependent carbamoyl-phosphate synthase. Glutamine-dependent carbamyl phosphate synthetase.":496,"Carbamoyl-phosphate synthase (glutamine-hydrolyzing).":496,"protein serine/threonine phosphatase activity":496,"thymidylate synthase activity":496,"fatty acid elongation":495,"insulin receptor binding":495,"positive regulation of peptide hormone secretion":495,"42-meric":494,"Cytochrome b-c1 complex subunit Rieske, mitochondrial":494,"60S RIBOSOMAL PROTEIN L2-A":493,"Heat shock protein HSP 90-alpha":493,"Histone H2B 1.1":493,"Hsp70 protein binding":493,"Hypothetical protein":493,"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)":493,"SUGAR (BETA-D-GALACTOSE)":493,"Soluble acetylcholine receptor":493,"Triosephosphate isomerase":493,"30S Ribosomal Protein THX":492,"Glutamate dehydrogenase (NAD(P)(+)).":492,"L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H.":492,"metabolic process":492,"negative regulation of protein complex assembly":492,"protein import into mitochondrial outer membrane":492,"Xanthine dehydrogenase/oxidase":491,"regulation of Golgi inheritance":491,"3',5'-cyclic-GMP phosphodiesterase activity":490,"A phosphate monoester + H(2)O = an alcohol + phosphate.":490,"Coat protein":490,"Escherichia coli (strain K12)":490,"lipoprotein transport":490,"tubulin binding":490,"-!- This enzyme catalyzes the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules, which may be either guanosine or adenosine. -!- This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. -!- The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine. -!- Formerly EC 2.1.1.58.":489,"Cap1-MTase. mRNA (nucleoside-2'-O)-methyltransferase.":489,"FRUIT FLY":489,"Methyltransferase cap1.":489,"Pisum sativum":489,"S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)- (purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)- methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)- [mRNA].":489,"postsynapse":489,"thiol-dependent ubiquitin-specific protease activity":489,"Acetylcholine-binding protein":488,"Pyrococcus abyssi GE5":488,"negative regulation of JUN kinase activity":488,"phosphatidylinositol binding":488,"positive regulation of vascular endothelial growth factor receptor signaling pathway":488,"regulation of signal transduction":488,"Lymnaea stagnalis":487,"negative regulation of receptor biosynthetic process":487,"telomeric DNA binding":487,"Fructose-1,6-bisphosphatase 1":486,"neuron projection development":486,"single-species biofilm formation":486,"JAK-STAT cascade":485,"lipid homeostasis":485,"metalloaminopeptidase activity":485,"positive regulation of interferon-beta production":485,"protein acetylation":485,"(S)-malate + NAD(+) = oxaloacetate + NADH.":484,"-!- Also oxidizes some other 2-hydroxydicarboxylic acids.":484,"Catalase":484,"Malate dehydrogenase.":484,"Malic dehydrogenase.":484,"RIBOSOMAL PROTEIN L15":484,"U4/U6 x U5 tri-snRNP complex":484,"epidermal growth factor receptor binding":484,"Burkholderia cenocepacia J2315":483,"Nicotiana tabacum":483,"RIBOSOMAL PROTEIN L3":483,"immunological synapse":483,"2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID":482,"microtubule-based movement":482,"ATCC 25618 / H37Rv":481,"ATP synthase subunit beta":481,"white fat cell differentiation":481,"ANTIMICROBIAL PROTEIN":480,"H-2 class I histocompatibility antigen, D-B alpha chain":480,"SUGAR (9-MER)":480,"semaphorin-plexin signaling pathway":480,"ATP synthase subunit alpha":479,"B cell activation":479,"insulin receptor substrate binding":479,"negative regulation of release of cytochrome c from mitochondria":479,"immune system":478,"lyase":478,"positive regulation of vasoconstriction":478,"protein disulfide oxidoreductase activity":478,"Phosphorylase Kinase; domain 1":477,"digestion":477,"mitotic nuclear envelope disassembly":477,"negative regulation of sequestering of triglyceride":477,"BH10":476,"Glutaredoxin":476,"Hemoglobin beta chain":476,"Nitrogenase molybdenum-iron protein beta chain":476,"Deoxyuridine-triphosphatase. Desoxyuridine 5'-triphosphatase. Desoxyuridine 5'-triphosphate nucleotidohydrolase. dUTP pyrophosphatase. dUTPase.":475,"calcium-transporting ATPase activity":475,"dUTP + H(2)O = dUMP + diphosphate.":475,"dUTP diphosphatase.":475,"neurotrophin TRK receptor signaling pathway":475,"CL Brener":474,"liver development":474,"positive regulation of cytokinesis":474,"alditol:NADP+ 1-oxidoreductase activity":473,"positive regulation of epithelial cell migration":473,"Vibrio parahaemolyticus RIMD 2210633":472,"regulation of innate immune response":472,"Catalase-peroxidase":471,"DNA protection during starvation protein":471,"response to glucocorticoid":471,"response to ionizing radiation":471,"-!- Also acts on UDP-2-deoxyglucose.":470,"30S ribosomal protein THX":470,"DNA binding, bending":470,"RNA polymerase II core promoter sequence-specific DNA binding":470,"branching morphogenesis of an epithelial tube":470,"heart contraction":470,"polysome":470,"structural constituent of cytoskeleton":470,"NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.":469,"Phosphoric monoester hydrolases.":469,"Purine nucleoside phosphorylase":469,"lung development":469,"negative regulation of monocyte chemotactic protein-1 production":469,"pyruvate kinase activity":469,"regulation of cell differentiation":469,"viral DNA genome replication":469,"(1) Xanthine + NAD(+) + H(2)O = urate + NADH. (2) Hypoxanthine + NAD(+) + H(2)O = xanthine + NADH.":468,"-!- Acts on a variety of purines and aldehydes, including hypoxanthine. -!- The mammalian enzyme can also convert all-trans retinol to all-trans- retinoate, while the substrate is bound to a retinoid-binding protein. -!- The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum center. -!- The mammallian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). -!- During purification the enzyme is largely converted to an O(2)- dependent form, EC 1.17.3.2. -!- The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion. -!- The conversion can also occur in vivo. -!- Formerly EC 1.2.1.37 and EC 1.1.1.204.":468,"Bacillus amyloliquefaciens":468,"N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE":468,"NAD-xanthine dehydrogenase. Xanthine oxidoreductase. Xanthine-NAD oxidoreductase. Xanthine/NAD(+) oxidoreductase.":468,"Xanthine dehydrogenase.":468,"positive regulation of glucose import":468,"DNA dealkylation involved in DNA repair":467,"L-ORNITHINE":467,"cofactor binding":467,"URIDINE-5'-MONOPHOSPHATE":466,"beta-catenin destruction complex disassembly":466,"ferroxidase activity":466,"negative regulation of cholesterol biosynthetic process":466,"Histone H3.1":465,"muscle filament sliding":465,"positive regulation of neuron differentiation":465,"positive regulation of tumor necrosis factor production":465,"Bacillus halodurans":464,"DNA damage response, signal transduction by p53 class mediator":464,"Insulin-degrading enzyme":464,"Lama glama":464,"1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL":463,"Arthrobacter globiformis":463,"BENZOIC ACID":463,"TRNA-FMET":463,"Transcription attenuation protein MtrB":463,"protein phosphatase 2A binding":463,"regulation of MAPK cascade":463,"Pseudomonas sp.":462,"T4 LYSOZYME":462,"-!- Also acts on 3-phospho-D-erythronate.":461,"-!- Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1. -!- Under some conditions the product is mainly superoxide rather than peroxide: R-H + H(2)O + 2 O(2) = ROH + 2 O(2)(.-) + 2 H(+). -!- The mammallian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4). -!- During purification the enzyme is largely converted to the O(2)- dependent xanthine oxidase form (EC 1.17.3.2). -!- The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion. -!- The conversion can also occur in vivo. -!- Formerly EC 1.1.3.22 and EC 1.2.3.2.":461,"2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.":461,"2-phosphoglycerate dehydratase. Enolase.":461,"HLA-B, HLAB":461,"Hypoxanthine oxidase. Hypoxanthine-xanthine oxidase. Schardinger enzyme. Xanthine oxidoreductase.":461,"Phosphopyruvate hydratase.":461,"Xanthine + H(2)O + O(2) = urate + H(2)O(2).":461,"Xanthine oxidase.":461,"drug metabolic process":461,"(1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O.":460,"-!- Belongs to peptidase family M27.":460,"-!- Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site. -!- In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.":460,"ATCC 35092 / DSM 1617 / JCM 11322 / P2":460,"Catalase peroxidase.":460,"N315":460,"beta-catenin destruction complex":460,"regulation of catalytic activity":460,"response to UV":460,"ribonuclease activity":459,"COBALT HEXAMMINE(III)":458,"Ferritin":458,"Hydro-lyases.":458,"Malate dehydrogenase":458,"cellular response to glucagon stimulus":458,"proline-rich region binding":458,"-!- The alpha-subunit catalyzes the conversion of 1-C-(indol-3- yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8). -!- The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. -!- In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24. -!- In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). -!- That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.":457,"Indoleglycerol phosphate aldolase. L-tryptophan synthetase. Tryptophan desmolase. Tryptophan synthetase.":457,"L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.":457,"STIGMATELLIN A":457,"Tryptophan synthase.":457,"mRNA 3'-end processing":457,"peptide cross-linking":457,"phosphatidylinositol 3-kinase binding":457,"Peroxidases.":456,"negative regulation of lipid storage":456,"Aspartate aminotransferase":455,"positive regulation of cholesterol biosynthetic process":455,"response to amino acid":455,"spindle pole centrosome":455,"4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE":454,"ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE":454,"Human immunodeficiency virus type 1 (BRU ISOLATE)":454,"cognition":454,"cytokine binding":454,"fibroblast growth factor-activated receptor activity":454,"DNA-directed RNA polymerase alpha chain":453,"SULFITE ION":453,"basal lamina":453,"protein poly-ADP-ribosylation":453,"protein serine/threonine kinase activator activity":453,"-!- Acts both as a dioxygenase and as a peroxidase.":452,"Arachidonate + AH(2) + 2 O(2) = prostaglandin H(2) + A + H(2)O.":452,"PG synthetase. Prostaglandin G/H synthase. Prostaglandin synthase. Prostaglandin synthetase.":452,"Prostaglandin-endoperoxide synthase.":452,"activation of signaling protein activity involved in unfolded protein response":452,"cell morphogenesis":452,"positive regulation of osteoblast proliferation":452,"prostaglandin-endoperoxide synthase activity":452,"protein phosphatase 2B binding":452,"threonine-type endopeptidase activity":452,"translation repressor activity, nucleic acid binding":452,"vitamin D receptor signaling pathway":452,"L-lactate dehydrogenase A chain":451,"catalytic activity":451,"glycogen metabolic process":451,"insulin metabolic process":451,"sequence-specific mRNA binding":451,"actin filament organization":450,"bovine,cow,domestic cattle,domestic cow":450,"methylation":450,"purine-containing compound salvage":450,"regulation of protein complex assembly":450,"regulation of response to DNA damage stimulus":450,"TRANSFERASE/RNA":449,"hydrogen peroxide biosynthetic process":449,"protein localization to plasma membrane":449,"MRE-600":448,"male gonad development":448,"3',5'-cyclic-GMP phosphodiesterase.":447,"Bacillus subtilis subsp. subtilis":447,"Bacteroides fragilis NCTC 9343":447,"Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate.":447,"HXB2 ISOLATE":447,"HYDROLASE-HYDROLASE INHIBITOR complex":447,"VIRUS/RNA":447,"cellular response to growth factor stimulus":447,"learning":447,"modification-dependent protein catabolic process":447,"nonadecameric":447,"positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway":447,"Mu50":446,"cell cycle G1/S phase transition":446,"neural tube closure":446,"octadecameric":446,"regulation of bone resorption":446,"Aminoacyltransferases.":445,"OXIDOREDUCTASE, NITRIC OXIDE SYNTHASE, INHIBITOR COMPLEX":445,"Polyprotein":445,"Synechocystis sp.":445,"angiogenesis involved in wound healing":445,"cellular calcium ion homeostasis":445,"cortical cytoskeleton":445,"positive regulation of lipid storage":445,"Xenopus":444,"ribosome 50S, PROTEIN-PROTEIN COMPLEX, RNA-RNA COMPLEX, PROTEIN-RNA COMPLEX, PEPTIDYL TRANSFERASE REACTION, RIBOSOME":444,"1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE":443,"GUANIDINE":443,"Hemoglobin alpha chain":443,"Nitrogenase molybdenum-iron protein alpha chain":443,"Urokinase-type plasminogen activator":443,"catalytic complex":443,"internal peptidyl-lysine acetylation":443,"negative regulation of cell cycle":443,"DNA polymerase lambda":442,"Escherichia coli CFT073":442,"Helicobacter":442,"-!- Also acts on dATP to form 3',5'-cyclic dAMP. -!- Requires pyruvate. -!- Activated by NAD(+) in presence of EC 2.4.2.31.":441,"3',5'-cyclic AMP synthetase. Adenyl cyclase. Adenylyl cyclase. ATP pyrophosphate-lyase.":441,"6,7-dimethyl-8-ribityllumazine synthase":441,"ATP = 3',5'-cyclic AMP + diphosphate.":441,"Adenylate cyclase.":441,"COL":441,"DNA-directed RNA polymerase beta chain":441,"Replicase polyprotein 1a":441,"positive regulation of cell-matrix adhesion":441,"-!- The enzyme, which participates in the degradation of aromatic compounds, catalyzes the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring. -!- The type of cleavage leads to mineralization via the intermediate 3-oxoadipate. -!- Formerly EC 1.13.1.3 and EC 1.99.2.3.":440,"3,4-dihydroxybenzoate + O(2) = 3-carboxy-cis,cis-muconate.":440,"C58":440,"Proteasome subunit alpha type-7":440,"Protocatechuate 3,4-dioxygenase.":440,"Protocatechuate oxygenase.":440,"erythrocyte differentiation":440,"C3HC4-type RING finger domain binding":439,"Staphylococcus aureus subsp. aureus MRSA252":439,"apoplast":439,"positive regulation of viral entry into host cell":439,"spindle assembly":439,"-!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7.":438,"Aldolase. D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Fructose-1,6-bisphosphate triosephosphate-lyase.":438,"Campylobacter jejuni":438,"D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.":438,"Fructose-bisphosphate aldolase.":438,"Rhodococcus erythropolis":438,"Thermoplasma":438,"integral component of endoplasmic reticulum membrane":438,"mRNA catabolic process":438,"positive regulation of G-protein coupled receptor protein signaling pathway":438,"regulation of osteoblast differentiation":438,"Desulfovibrio vulgaris str. Hildenborough":437,"activation of innate immune response":437,"positive regulation of excitatory postsynaptic potential":437,"suppression by virus of host NF-kappaB transcription factor activity":437,"suppression by virus of host type I interferon-mediated signaling pathway":437,"transport vesicle":437,"Aurora kinase A":436,"BETA-GALACTOSIDASE":436,"HEXANE-1,6-DIOL":436,"Rho protein signal transduction":436,"Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.":436,"myosin binding":436,"nickel cation binding":436,"positive regulation of epithelial to mesenchymal transition":436,"'de novo' pyrimidine nucleobase biosynthetic process":435,"Azurin":435,"Bacillus thermoproteolyticus":435,"DNA-directed RNA polymerase II subunit 9":435,"DNA-directed RNA polymerases I/II/III subunit 10":435,"PROTEIN (DNA POLYMERASE BETA (E.C.2.7.7.7))":435,"SACCHAROMYCES CEREVISIAE GENOMIC DNA CONTAINING ITS1,5.8S RRNA GENE, ITS2,28S RRNA GENE, STRAIN KW97":435,"Thermolysin":435,"negative regulation of interferon-gamma-mediated signaling pathway":435,"translation elongation factor activity":435,"L-aspartate:2-oxoglutarate aminotransferase activity":434,"autophagosome":434,"glutathione binding":434,"3C-like proteinase":433,"regulation of mitochondrial membrane permeability":433,"signal transducer, downstream of receptor, with protein tyrosine kinase activity":433,"triglyceride catabolic process":433,"Monomeric":432,"Peroxisome proliferator-activated receptor gamma":432,"Stmn4":432,"Synechococcus elongatus":432,"Thiolester hydrolases.":432,"apoptotic DNA fragmentation":432,"regulation of calcium ion transport":432,"response to low-density lipoprotein particle":432,"48-meric":431,"Integrin beta-3":431,"proteinaceous extracellular matrix":431,"-!- Requires calmodulin for activity. -!- The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. -!- For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. -!- The enzyme couples muscle contraction with energy production via glycogenolysis--glycolysis by catalyzing the Ca(2+)-dependent phosphorylation and activation of glycogen phosphorylase b. -!- The gamma subunit of the tetrameric alpha-beta-gamma-delta enzyme is the catalytic subunit. -!- Formerly EC 2.7.1.38.":430,"2 ATP + phosphorylase b = 2 ADP + phosphorylase a.":430,"Dephosphophosphorylase kinase. Glycogen phosphorylase kinase. PHK. Phosphorylase b kinase. Phosphorylase B kinase. Phosphorylase kinase (phosphorylating).":430,"GFP":430,"Hexosyltransferases.":430,"Phosphorylase kinase.":430,"epoxygenase P450 pathway":430,"fibroblast growth factor receptor binding":430,"inclusion body":430,"-!- Also hydrolyzes alpha-N-substituted L-arginines and canavanine.":429,"ASPARTIC ACID":429,"Arginase.":429,"Arginine amidinase. Canavanase.":429,"L-arginine + H(2)O = L-ornithine + urea.":429,"Proteasome subunit alpha":429,"S-adenosylmethionine catabolic process":429,"cell":429,"histone acetylation":429,"negative regulation of MAPK cascade":429,"-!- This multiunctional enzyme catalyzes both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes. -!- In addition, the enzyme also catalyzes EC 2.4.99.20. -!- Cf. EC 3.2.2.5.":428,"ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.":428,"HIV-1 M:B_ARV2/SF2":428,"NAD hydrolase. NAD(+) nucleosidase. NADase. Nicotinamide adenine dinucleotide nucleosidase.":428,"RIBOSOMAL PROTEIN L22":428,"Tubulin beta-2B chain":428,"-!- A thermostable extracellular metalloendopeptidase containing four calcium ions. -!- Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus and Aspergillus oryzae. -!- Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin. -!- Belongs to peptidase family M4. -!- Formerly EC 3.4.24.4.":427,"-!- In those organisms producing N-formylmethionyl-tRNA(fMet) for translation initiation, this enzyme also recognizes the initiator tRNA(fMet) and catalyzes the formation of L-methionyl-tRNA(fMet), the substrate for EC 2.1.2.9.":427,"-!- This family of enzymes can phosphorylate both Ser/Thr and Tyr residues. -!- Formerly EC 2.7.1.37.":427,"ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl- tRNA(Met).":427,"Bacillus thermoproteolyticus neutral proteinase.":427,"Dual-specificity kinase.":427,"Flavivirin.":427,"HISTIDINE":427,"Methionine translase. Methionyl-transfer ribonucleate synthetase. Methionyl-transfer ribonucleic acid synthetase. Methionyl-transfer RNA synthetase. Methionyl-tRNA synthetase. MetRS.":427,"Methionine--tRNA ligase.":427,"NS2B-3 proteinase. Yellow fever virus protease.":427,"Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.":427,"Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.":427,"Thermolysin.":427,"Trypsin-like serine proteases":427,"learning or memory":427,"apolipoprotein A-I-mediated signaling pathway":426,"-!- Also catalyzes the anomerization of D-glucose 6-phosphate.":425,"D-glucose 6-phosphate = D-fructose 6-phosphate.":425,"DNA topological change":425,"Glucose-6-phosphate isomerase.":425,"Hexose monophosphate isomerase. Hexosephosphate isomerase. Oxoisomerase. Phosphoglucoisomerase. Phosphoglucose isomerase. Phosphohexoisomerase. Phosphohexomutase. Phosphohexose isomerase. Phosphosaccharomutase.":425,"Lactobacillus":425,"low-density lipoprotein particle receptor biosynthetic process":425,"mitochondrial proton-transporting ATP synthase, catalytic core":425,"prostaglandin receptor activity":425,"Acting on peptide bonds (peptidases).":424,"Antigen-presenting glycoprotein CD1d1":424,"CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE":424,"Coronavirus":424,"MC58":424,"Pyrobaculum aerophilum str. IM2":424,"cell leading edge":424,"positive regulation of protein metabolic process":424,"ubiquitin homeostasis":424,"Hordeum vulgare":423,"Wnt signaling pathway, calcium modulating pathway":423,"cilium":423,"nucleosome":423,"positive regulation of cell differentiation":423,"regulation of cellular protein localization":423,"response to radiation":423,"Dimeric":422,"HYDROXIDE ION":422,"K1":422,"carbamoyl-phosphate synthase complex":422,"establishment of protein localization to membrane":422,"low-density lipoprotein particle receptor binding":422,"regulation of extrinsic apoptotic signaling pathway via death domain receptors":422,"response to bacterium":422,"vascular endothelial growth factor receptor 2 binding":422,"50S Ribosomal Protein L18":421,"Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial":421,"adherens junction organization":421,"placenta development":421,"regulation of smooth muscle cell migration":421,"regulation of telomere maintenance":421,"-!- The pancreatic enzyme acts only on an ester-water interface; the outer ester links are preferentially hydrolyzed.":420,"-!- This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14. -!- Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314). -!- In the archaeon Pyrococcus horikoshii the enzyme acts on His(600) of elongation factor 2.":420,"3 S-adenosyl-L-methionine + 2-((3S)-3-carboxy-3-aminopropyl)-L-histidine- [translation elongation factor 2] = 3 S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2].":420,"Aspergillus":420,"Coxiella burnetii RSA 493":420,"Cytochrome c-552":420,"Diphthine synthase":420,"Diphthine synthase.":420,"Glutamate dehydrogenase 1, mitochondrial":420,"L-lactate dehydrogenase":420,"Lipase. Tributyrase. Triglyceride lipase.":420,"Triacylglycerol + H(2)O = diacylglycerol + a carboxylate.":420,"Triacylglycerol lipase.":420,"adherens junction":420,"biotin biosynthetic process":420,"cellular response to dexamethasone stimulus":420,"negative regulation of GTPase activity":420,"syntaxin binding":420,"50S Ribosomal Protein L13":419,"50S Ribosomal Protein L14":419,"50S Ribosomal Protein L15":419,"50S Ribosomal Protein L16":419,"50S Ribosomal Protein L17":419,"50S Ribosomal Protein L19":419,"50S Ribosomal Protein L2":419,"50S Ribosomal Protein L20":419,"50S Ribosomal Protein L21":419,"50S Ribosomal Protein L22":419,"50S Ribosomal Protein L23":419,"50S Ribosomal Protein L24":419,"50S Ribosomal Protein L25":419,"50S Ribosomal Protein L27":419,"50S Ribosomal Protein L28":419,"50S Ribosomal Protein L29":419,"50S Ribosomal Protein L3":419,"50S Ribosomal Protein L30":419,"50S Ribosomal Protein L31":419,"50S Ribosomal Protein L32":419,"50S Ribosomal Protein L33":419,"50S Ribosomal Protein L34":419,"50S Ribosomal Protein L35":419,"50S Ribosomal Protein L4":419,"50S Ribosomal Protein L5":419,"50S Ribosomal Protein L6":419,"50S Ribosomal Protein L9":419,"DNA-directed RNA polymerase beta' chain":419,"nuclear-transcribed mRNA poly(A) tail shortening":419,"positive regulation of glucose transport":419,"telomere maintenance via recombination":419,"telomere organization":419,"uncultured bacterium":419,"BIOTIN":418,"Brevibacterium fuscum":418,"Chaetomium thermophilum var. thermophilum DSM 1495":418,"Clostridium perfringens":418,"DIOXOTHIOMOLYBDENUM(VI) ION":418,"Dickeya chrysanthemi":418,"Homoprotocatechuate 2,3-dioxygenase":418,"Methylococcus capsulatus str. Bath":418,"RNA polymerase II transcription coactivator activity":418,"filopodium membrane":418,"negative regulation of lipid transport":418,"regulation of microtubule-based process":418,"visual perception":418,"Bacillus virus phi29":417,"Chicken":417,"Oryctolagus":417,"regulation of membrane potential":417,"regulation of synaptic plasticity":417,"Lactotransferrin":416,"NEOMYCIN":416,"epidermis development":416,"positive regulation of phospholipase C activity":416,"regulation of protein binding":416,"regulation of triglyceride biosynthetic process":416,"DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11":415,"DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2":415,"DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3":415,"DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9":415,"Fab heavy chain":415,"TRAF2-GSTP1 complex":415,"positive regulation of brown fat cell differentiation":415,"prostaglandin metabolic process":415,"protein K48-linked ubiquitination":415,"suppression by virus of host IRF3 activity by inhibition of IRF3 phosphorylation":415,"1710b":414,"Bontoxilysin.":414,"Botulinum neurotoxin.":414,"Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.":414,"NOS3":414,"RNA metabolic process":414,"TIM BARREL (ALPHA/BETA BARREL), JELLY-ROLL BARREL, IMMUNOGLOBULIN, BETA SUPERSANDWICH, HYDROLASE":414,"cysteine-type endopeptidase activity involved in apoptotic process":414,"negative regulation of fatty acid biosynthetic process":414,"syntaxin-1 binding":414,"C5L2 anaphylatoxin chemotactic receptor binding":413,"HYDROLASE/TRANSPORT PROTEIN":413,"Streptomyces lividans":413,"cell body":413,"histone methylation":413,"triose-phosphate isomerase activity":413,"NuRD complex":412,"diphthine synthase activity":412,"negative regulation of synaptic transmission, glutamatergic":412,"potassium channel regulator activity":412,"regulation of actin cytoskeleton reorganization":412,"regulation of centrosome cycle":412,"(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)- 9,10-dihydroxyoctadecanoate + phosphate.":411,"-!- The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10. -!- The best substrates for this enzyme are 10-hydroxy-9- (phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form. -!- The phosphatase activity is not found in plant EC 3.3.2.10 or in mammalian EC 3.3.2.9.":411,"Bifunctional epoxide hydrolase 2":411,"Candida albicans":411,"Dihydroxy fatty acid phosphatase. Hydroxy fatty acid phosphatase. Hydroxy lipid phosphatase. Soluble epoxide hydrolase.":411,"Lipid-phosphate phosphatase.":411,"Transferring alkyl or aryl groups, other than methyl groups.":411,"biotin carboxylase activity":411,"cholesterol metabolic process":411,"negative regulation of interleukin-1 beta production":411,"Methanosarcina mazei Go1":410,"Neisseria":410,"cellular response to amino acid stimulus":410,"long-chain fatty acid biosynthetic process":410,"positive regulation of macroautophagy":410,"skeletal system morphogenesis":410,"P-site tRNA fMet":409,"Pseudomonas stutzeri":409,"RNA 7-methylguanosine cap binding":409,"SUGAR (ALPHA-L-FUCOSE)":409,"cAMP biosynthetic process":409,"regulation of focal adhesion assembly":409,"Fibrinogen beta chain":408,"Nitric oxide synthase, inducible":408,"SYNTHETIC CONSTRUCT":408,"Thrombin heavy chain":408,"Vibrio parahaemolyticus":408,"TETRAETHYLAMMONIUM ION":407,"intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress":407,"monooxygenase activity":407,"negative regulation of DNA damage checkpoint":407,"-!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC 3.4.1.1.":406,"Cadherins":406,"Cytosol aminopeptidase. Leucine aminopeptidase. Peptidase S.":406,"DNA replication-dependent nucleosome assembly":406,"DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 1":406,"Leucyl aminopeptidase.":406,"Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.":406,"TPA_INF\\: SACCHAROMYCES CEREVISIAE S288C CHROMOSOME XII, COMPLETE SEQUENCE":406,"complement activation, lectin pathway":406,"negative regulation of hydrogen peroxide-mediated programmed cell death":406,"positive regulation of glycogen biosynthetic process":406,"regulation of I-kappaB kinase/NF-kappaB signaling":406,"translation":406,"Bromodomain-containing protein 4":405,"Ensifer meliloti":405,"N-{(2S)-2-[(MORPHOLIN-4-YLACETYL)AMINO]-4-PHENYLBUTANOYL}-L-LEUCYL-N-[(2R,3S,4S)-1,3-DIHYDROXY-2,6-DIMETHYLHEPTAN-4-YL]-L-PHENYLALANINAMIDE":405,"P-site tRNA":405,"chromatin assembly":405,"positive regulation of cell-substrate adhesion":405,"-!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.15 and EC 3.4.99.19.":404,"-!- The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. -!- In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage. -!- Formerly EC 6.3.2.19.":404,"Angiotensin-forming enzyme. Angiotensinogenase.":404,"Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.":404,"E2 ubiquitin-conjugating enzyme.":404,"Hemagglutinin HA2":404,"Renin.":404,"S-1,2-PROPANEDIOL":404,"S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine.":404,"Ubiquitin-carrier-protein E2. Ubiquitin-conjugating enzyme E2.":404,"cAMP catabolic process":404,"cellular response to hepatocyte growth factor stimulus":404,"COENZYME Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-ISOMER":403,"Cytochrome c oxidase subunit 6B1":403,"Cytochrome c oxidase subunit 6C":403,"DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3":403,"DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4":403,"DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5":403,"KOD1":403,"Nuclear receptor coactivator 2":403,"intercalated disc":403,"peptide antigen assembly with MHC class II protein complex":403,"peroxiredoxin activity":403,"positive regulation of T cell activation":403,"protein kinase CK2 complex":403,"-!- Large group of enzymes which recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition site. -!- See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/":402,"-!- The animal enzyme requires acetyl-CoA.":402,"50S ribosomal protein L7/L12":402,"ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate.":402,"CENP-A containing nucleosome assembly":402,"Cryptosporidium parvum Iowa II":402,"Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.":402,"Hemagglutinin HA1":402,"NUCLEOTIDYLTRANSFERASE":402,"Pyruvate carboxylase.":402,"Pyruvic carboxylase.":402,"RNA polymerase sigma factor RpoD":402,"Type II restriction enzyme.":402,"Type II site-specific deoxyribonuclease.":402,"axonogenesis":402,"cytoplasmic ribonucleoprotein granule":402,"negative regulation of transcription from RNA polymerase II promoter in response to hypoxia":402,"SUGAR (GLUCOSE)":401,"bradykinin catabolic process":401,"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen":401,"positive regulation of interferon-alpha production":401,"-!- Cytosolic enzyme, known from mammals and Drosophila melanogaster. -!- Inhibited by bacitracin, chelating agents EDTA and 1,10- phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not by phosphoramidon. -!- Belongs to peptidase family M16. -!- Formerly EC 3.4.22.11, EC 3.4.99.10 and EC 3.4.99.45.":400,"CHOLESTEROL":400,"DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1":400,"Degradation of insulin, glucagon and other polypeptides. No action on proteins.":400,"Fab light chain":400,"Insulin protease. Insulin-degrading enzyme. Insulinase.":400,"Insulysin.":400,"positive regulation of B cell differentiation":400,"protein deacetylation":400,"Beta-Galactosidase":399,"CYTIDINE-5'-MONOPHOSPHATE":399,"FAB FRAGMENT":399,"MLL1 complex":399,"NITRITE ION":399,"SOS response":399,"Triticum aestivum":399,"protein kinase A catalytic subunit binding":399,"(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE":398,"-!- Formed from the inactive precursor by action of plasmin or plasma kallikrein. -!- Differs in structure from EC 3.4.21.68, and does not bind to fibrin. -!- Belongs to peptidase family S1. -!- Formerly EC 3.4.21.31 and EC 3.4.99.26.":398,"-!- Involved in riboflavin biosynthesis.":398,"-!- Involved with EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide.":398,"-!- This multiunctional enzyme catalyzes both the removal of nicotinamide from NADP(+), forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming NAADP(+), a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes. -!- In addition, the enzyme also catalyzes EC 3.2.2.6.":398,"1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6- (D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H(2)O + phosphate.":398,"2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase.":398,"6,7-dimethyl-8-ribityllumazine synthase.":398,"ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.":398,"Alanine:alanine ligase (ADP-forming). Alanylalanine synthetase. D-Ala-D-Ala synthetase. D-alanyl-D-alanine synthetase. D-alanylalanine synthetase.":398,"Caulobacter crescentus CB15":398,"Cellular plasminogen activator. Urinary plasminogen activator. Urokinase.":398,"Clostridioides difficile 630":398,"D-alanine--D-alanine ligase.":398,"Diphosphopyridine nucleosidase.":398,"H-2 class I histocompatibility antigen, K-B alpha chain":398,"Lumazine synthase.":398,"NADP(+) + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide.":398,"U-plasminogen activator.":398,"-!- Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. -!- Not identical with EC 2.5.1.51, EC 2.5.1.52 and EC 2.5.1.53. -!- Formerly EC 4.2.99.8.":397,"Acetyl-CoA acetyltransferase":397,"Acetylserine sulfhydrylase. Cysteine synthetase. O(3)-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide). O-acetyl-L-serine sulfhydrylase. O-acetyl-L-serine sulfohydrolase. O-acetylserine (thiol)-lyase. O-acetylserine (thiol)-lyase A. O-acetylserine sulfhydrylase. OAS sulfhydrylase.":397,"Brucella abortus 2308":397,"Cysteine synthase.":397,"N-glycan processing":397,"O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.":397,"RAT":397,"brush border":397,"chloroplast envelope":397,"glutamine biosynthetic process":397,"heparan sulfate proteoglycan binding":397,"leukotriene biosynthetic process":397,"regulation of acetyl-CoA biosynthetic process from pyruvate":397,"tRNA export from nucleus":397,"-!- Involved in the synthesis of glycoproteins.":396,"ATP-dependent DNA helicase activity":396,"RNA polymerase II distal enhancer sequence-specific DNA binding":396,"cellular response to organic substance":396,"insulin catabolic process":396,"regulation of mitotic spindle assembly":396,"-!- Specificity varies with the source and with the activating metal ion. -!- The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9.":395,"Diphosphate + H(2)O = 2 phosphate.":395,"Diphosphate phosphohydrolase. Inorganic pyrophosphatase. Pyrophosphate phosphohydrolase.":395,"E-site tRNA":395,"Inorganic diphosphatase.":395,"Pancreatic trypsin inhibitor":395,"Renin":395,"Streptococcus pyogenes serotype M1":395,"negative regulation of biosynthetic process":395,"negative regulation of protein homooligomerization":395,"positive regulation of execution phase of apoptosis":395,"proton-transporting ATPase activity, rotational mechanism":395,"3-oxoacyl-[acyl-carrier-protein] synthase activity":394,"Pyruvate carboxylase":394,"RIBOSOMAL PROTEIN L24":394,"RIBOSOMAL PROTEIN L37E":394,"Thrombin light chain":394,"nuclear heterochromatin":394,"platelet formation":394,"tetrahydrofolate biosynthetic process":394,"Camelus dromedarius":393,"Clostridium thermocellum":393,"DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 2":393,"Immune system":393,"Synechocystis":393,"adenylate cyclase activity":393,"extracellular domain":393,"groEL protein":393,"regulation of smooth muscle cell-matrix adhesion":393,"293":392,"ATP-dependent RNA helicase activity":392,"Moorella thermoacetica":392,"Pseudomonas putida KT2440":392,"-!- The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. -!- The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. -!- Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition. -!- Formerly EC 2.7.7.21 and EC 2.7.7.25.":391,"A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.":391,"CCA tRNA nucleotidyltransferase.":391,"CCA-adding enzyme. Ribonucleic cytidylic cytidylic adenylic pyrophosphorylase. Transfer ribonucleic adenylyl (cytidylyl) transferase. Transfer RNA adenylyltransferase. Transfer-RNA nucleotidyltransferase. tRNA adenylyl(cytidylyl)transferase. tRNA CCA-diphosphorylase. tRNA cytidylyltransferase. tRNA-nucleotidyltransferase.":391,"DNA strand elongation involved in DNA replication":391,"E":391,"MITOCHONDRIA":391,"Nitrosomonas europaea ATCC 19718":391,"PANCREAS":391,"Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial":391,"THYMIDINE-3',5'-DIPHOSPHATE":391,"chaperone cofactor-dependent protein refolding":391,"lipid phosphatase activity":391,"phosphorelay signal transduction system":391,"CESIUM ION":390,"DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4":390,"ELONGATION FACTOR TU":390,"LIPID TRANSPORT":390,"PHOSPHOENOLPYRUVATE":390,"dihydrofolate reductase activity":390,"humoral immune response":390,"programmed cell death":390,"ubiquitin conjugating enzyme binding":390,"ALANINE":389,"LB400":389,"PCC 6803":389,"Pyrobaculum aerophilum":389,"Thermococcus kodakarensis":389,"dbh, dpo4, SSO2448":389,"ionotropic glutamate receptor signaling pathway":389,"negative regulation of telomere maintenance via telomerase":389,"positive regulation of NF-kappaB import into nucleus":389,"ALUMINUM FLUORIDE":388,"Aspartate carbamoyltransferase catalytic chain":388,"HB8 / ATCC 27634 / DSM 579":388,"PEP carboxykinase. PEPCK. Phosphoenolpyruvate carboxykinase. Phosphoenolpyruvate carboxylase. Phosphopyruvate carboxylase.":388,"PHOSPHOTRANSFERASE":388,"Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial":388,"chromosome, centromeric region":388,"glutamate binding":388,"mitochondrial envelope":388,"positive regulation of intracellular signal transduction":388,"tetrahydrobiopterin binding":388,"-!- P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- This enzyme family comprises three types of Ca(2+)-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in Saccharomyces cerevisiae. -!- The first and third transport one ion per ATP hydrolyzed, whereas the second transports two ions. -!- Formerly EC 3.6.1.38.":387,"ALLERGEN":387,"ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate + Ca(2+)(Side 2).":387,"Bacillus circulans":387,"Burkholderia thailandensis":387,"Ca(2+)-transporting ATPase. Calcium pump. Calcium-translocating P-type ATPase.":387,"Calcium-transporting ATPase.":387,"phospholipid dephosphorylation":387,"platelet alpha granule membrane":387,"replicative senescence":387,"stilbene catabolic process":387,"transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding":387,"EF-hand":386,"PHYCOCYANOBILIN":386,"YTTERBIUM (III) ION":386,"regulation of mitophagy":386,"-!- Catalyzes the oxidative deamination of neurotransmitters and biogenic amines. -!- Acts on primary amines, and also on some secondary and tertiary amines. -!- It differs from EC 1.4.3.21, as it can oxidize secondary and tertiary amines but not methylamine. -!- Inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22, it is not inhibited by semicarbazide. -!- Formerly EC 1.4.3.9.":385,"3[N-MORPHOLINO]PROPANE SULFONIC ACID":385,"Adrenaline oxidase. Amine oxidase. Amine oxidase (flavin-containing). Tyraminase. Tyramine oxidase.":385,"Monoamine oxidase.":385,"PCC 7942":385,"RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + H(2)O(2).":385,"Ribosomal protein eL13":385,"Ribosomal protein eL14":385,"Ribosomal protein eL15":385,"Ribosomal protein eL18":385,"Ribosomal protein eL19":385,"Ribosomal protein eL20":385,"Ribosomal protein eL21":385,"Ribosomal protein eL22":385,"Ribosomal protein eL24":385,"Ribosomal protein eL27":385,"Ribosomal protein eL28":385,"Ribosomal protein eL29":385,"Ribosomal protein eL30":385,"Ribosomal protein eL31":385,"Ribosomal protein eL32":385,"Ribosomal protein eL33":385,"Ribosomal protein eL34":385,"Ribosomal protein eL36":385,"Ribosomal protein eL37":385,"Ribosomal protein eL38":385,"Ribosomal protein eL39":385,"Ribosomal protein eL40":385,"Ribosomal protein eL41":385,"Ribosomal protein eL42":385,"Ribosomal protein eL43":385,"Ribosomal protein eL6":385,"Ribosomal protein eL8":385,"Ribosomal protein uL13":385,"Ribosomal protein uL14":385,"Ribosomal protein uL15":385,"Ribosomal protein uL16":385,"Ribosomal protein uL18":385,"Ribosomal protein uL22":385,"Ribosomal protein uL23":385,"Ribosomal protein uL24":385,"Ribosomal protein uL29":385,"Ribosomal protein uL3":385,"Ribosomal protein uL30":385,"Ribosomal protein uL4":385,"Ribosomal protein uL5":385,"Ribosomal protein uL6":385,"insulin-like growth factor receptor signaling pathway":385,"mesodermal cell differentiation":385,"microvillus membrane":385,"negative regulation of cell adhesion":385,"negative regulation of viral entry into host cell":385,"spindle midzone":385,"Calcium-gated potassium channel MthK":384,"Enterobacteria phage T7":384,"Ig gamma-1 chain C region":384,"positive regulation of IRE1-mediated unfolded protein response":384,"regulation of phosphorylation of RNA polymerase II C-terminal domain":384,"xanthine dehydrogenase complex":384,"-!- The enzyme associates with the spindle pole during mitosis and is thought to play an important role in the dynamic function of the mitotic spindle during chromosome segregation. -!- The human form of the enzyme, Plk1, does not phosphorylate histone H1, enolase and phosvitin but it can phosphorylate myelin basic protein and microtubule-associated protein MAP-2, although to a lesser extent than casein. -!- Formerly EC 2.7.1.37.":383,"Ames":383,"DNA-dependent ATPase activity":383,"Klebsiella":383,"NCTC 8325":383,"PLK. Polo serine-threonine kinase. Polo-like kinase.":383,"Polo kinase.":383,"SNARE binding":383,"Thioredoxin":383,"Transcription":383,"URIDINE-5'-DIPHOSPHATE-GLUCOSE":383,"extrinsic component of external side of plasma membrane":383,"muscle organ development":383,"protein complex scaffold":383,"BOVINE":382,"CATTLE":382,"Caldanaerobacter subterraneus subsp. tengcongensis MB4":382,"positive regulation of granulocyte macrophage colony-stimulating factor production":382,"-!- Deoxyuridine can also act as acceptor. -!- dGTP can also act as donor. -!- The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyzes this reaction as well as those of EC 2.7.1.114, EC 2.7.1.118, and EC 2.7.4.9. -!- Formerly EC 2.7.1.75.":381,"-!- The reduction of O(2) to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. -!- Several bacteria appear to contain analogous oxidases.":381,"4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O.":381,"ATP + thymidine = ADP + thymidine 5'-phosphate.":381,"Complex IV (mitochondrial electron transport). Cytochrome a3. Cytochrome aa3. Cytochrome oxidase. Warburg's respiratory enzyme.":381,"Cytochrome-c oxidase.":381,"Sin3 complex":381,"TRIS(HYDROXYETHYL)AMINOMETHANE":381,"Thymidine kinase.":381,"chromatin DNA binding":381,"mannosidase activity":381,"An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADPH.":380,"Glucose-6-phosphate isomerase":380,"Gria2, Glur2":380,"HYDROGEN PEROXIDE":380,"negative regulation of cysteine-type endopeptidase activity":380,"Corynebacterium diphtheriae NCTC 13129":379,"ERBB signaling pathway":379,"Lectin":379,"Paracoccus denitrificans PD1222":379,"Phosphotransferases with a nitrogenous group as acceptor.":379,"calcium channel complex":379,"carboxylic acid binding":379,"histone kinase activity (H3-T11 specific)":379,"negative regulation of cell-substrate adhesion":379,"negative regulation of protein kinase B signaling":379,"nucleic acid binding":379,"positive regulation of macrophage activation":379,"25618":378,"BARIUM ION":378,"DNA strand renaturation":378,"HEART":378,"LIGASE/RNA":378,"R1":378,"TRYPSIN":378,"U5 snRNP":378,"connexin binding":378,"malaria parasite P. falciparum":378,"phosphatidylserine binding":378,"Ig kappa chain C region":377,"enoyl-[acyl-carrier-protein] reductase (NADH) activity":377,"postreplication repair":377,"Bacteroides fragilis":376,"Histone H3":376,"Hydrolase/Hydrolase inhibitor":376,"Leishmania mexicana":376,"Macrophage migration inhibitory factor":376,"Nucleoprotein":376,"cell migration involved in sprouting angiogenesis":376,"lysine catabolic process":376,"negative regulation of helicase activity":376,"nuclear euchromatin":376,"positive regulation of fibrinolysis":376,"regulation of cardiac conduction":376,"Bacteroides":375,"Histone H2A type 1-B/E":375,"Histone H2B type 1-J":375,"U1 snRNP":375,"Wnt signalosome":375,"acute-phase response":375,"brown fat cell differentiation":375,"extracellular matrix binding":375,"phospholipase activator activity":375,"-!- Requires at least a dipeptide for an efficient rate of reaction. -!- N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. -!- Differs in substrate specificity from EC 3.5.1.27 and EC 3.5.1.31.":374,"50S Ribosomal Protein L36":374,"Fibrinogen gamma chain":374,"Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide.":374,"HEMAGGLUTININ":374,"Hepatitis C virus (isolate BK)":374,"PDF. Polypeptide deformylase.":374,"Peptide deformylase.":374,"STREPTOMYCIN":374,"entrainment of circadian clock":374,"thioesterase binding":374,"wound healing, spreading of epidermal cells":374,"DNA double-strand break processing":373,"L-tyrosine:2-oxoglutarate aminotransferase activity":373,"PLATINUM (II) ION":373,"Sarcoplasmic/endoplasmic reticulum calcium ATPase 1":373,"Structural polyprotein":373,"With NADH or NADPH as one donor, and incorporation of one atom of oxygen.":373,"negative regulation of mitotic nuclear division":373,"regulation of endothelial cell chemotaxis to fibroblast growth factor":373,"response to zinc ion":373,"29148":372,"COAT PROTEIN":372,"apical junction complex":372,"glutamate receptor activity":372,"glycine binding":372,"negative regulation of NF-kappaB transcription factor activity":372,"negative regulation of ubiquitin-protein transferase activity":372,"stress fiber":372,"DNA polymerase I":371,"L-lactate dehydrogenase activity":371,"Leucine-rich Repeat Variant":371,"OXYGEN ATOM":371,"PEROXIDE ION":371,"Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.":371,"bfrB, PA3531":371,"regulation of angiogenesis":371,"long-term memory":370,"metallocarboxypeptidase activity":370,"mitochondrial electron transport, ubiquinol to cytochrome c":370,"negative regulation of platelet aggregation":370,"positive regulation of platelet-derived growth factor receptor signaling pathway":370,"positive regulation of receptor internalization":370,"serine-type peptidase complex":370,"-!- The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. -!- Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12.":369,"GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate.":369,"GTP cyclohydrolase I.":369,"MUSCLE":369,"SUGAR (FRUCTOSE-6-PHOSPHATE)":369,"THIAMIN DIPHOSPHATE":369,"aggresome":369,"caveolin-mediated endocytosis":369,"-!- Also acts on other arylpyruvates.":368,"-!- In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. -!- This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. -!- In contrast, different enzymes are involved in the first reaction. -!- In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17. -!- In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157.":368,"ADENINE":368,"BADH. Betaine aldehyde dehydrogenase. Betaine aldehyde oxidase.":368,"Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH.":368,"Betaine-aldehyde dehydrogenase.":368,"Clostridium difficile":368,"HUMAN IMMUNODEFICIENCY VIRUS 1":368,"Keto-phenylpyruvate = enol-phenylpyruvate.":368,"Phenylpyruvate keto--enol tautomerase. Phenylpyruvic keto--enol isomerase.":368,"Phenylpyruvate tautomerase.":368,"Streptomyces clavuligerus":368,"V583":368,"miRNA metabolic process":368,"negative regulation of mitotic cell cycle":368,"regulation of podosome assembly":368,"ATCC 43587 / DSM 3638 / JCM 8422 / Vc1":367,"DNA primer":367,"MHC class I protein binding":367,"NUCLEAR PROTEIN":367,"bacterial-type RNA polymerase transcriptional activator activity, sequence-specific DNA binding":367,"nuc":367,"-!- The transforming growth factor beta (TGF-beta) family of cytokines regulates cell proliferation, differentiation, recognition and death. -!- Signaling occurs by the binding of ligand to the type II receptor, which is the constitutively active kinase. -!- Bound TGF-beta is then recognized by receptor I, which is phosphorylated and can propagate the signal to downstream substrates. -!- Formerly EC 2.7.1.37.":366,"3-dehydroquinate dehydratase activity":366,"ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.":366,"Activin receptor kinase. Receptor serine/threonine protein kinase. Receptor type I serine/threonine protein kinase. Receptor type II serine/threonine protein kinase. TGF-beta kinase.":366,"BILIVERDINE IX ALPHA":366,"E-SITE TRNA PHE OR P-SITE TRNA PHE":366,"FLAVOPROTEIN":366,"Klebsiella pneumoniae subsp. pneumoniae MGH 78578":366,"Major histocompatibility complex class I-related gene protein":366,"Mesorhizobium loti MAFF303099":366,"Receptor protein serine/threonine kinase.":366,"cleavage furrow":366,"histone methyltransferase activity":366,"peroxidase activity":366,"replicative cell aging":366,"(S)-dihydroorotate + fumarate = orotate + succinate.":365,"-!- Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP, 3',5'-cyclic GMP and 3',5'-cyclic CMP.":365,"-!- The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. -!- Molecular oxygen can replace fumarate in vitro. -!- Other class 1 dihydroorotate dehydrogenases use either NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor. -!- The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor. -!- Formerly EC 1.3.3.1.":365,"3',5'-cyclic-nucleotide phosphodiesterase.":365,"Cyclic AMP phosphodiesterase.":365,"DHOD. DHODase. DHOdehase. Dihydoorotic acid dehydrogenase. Dihydroorotate dehydrogenase. Dihydroorotate oxidase.":365,"DNA-DIRECTED DNA POLYMERASE, DNA REPLICATION, DNA REPAIR, NUCLEOTIDYLTRANSFERASE, COMPLEX (NUCLEOTIDYLTRANSFERASE-DNA, TRANSFERASE-DNA complex":365,"Dihydroorotate oxidase (fumarate).":365,"INOSINIC ACID":365,"Nucleoside 3',5'-cyclic phosphate + H(2)O = nucleoside 5'-phosphate.":365,"POLL":365,"cyclosporin A binding":365,"isomerase":365,"mRNA (guanine-N7-)-methyltransferase activity":365,"positive regulation of monocyte chemotaxis":365,"positive regulation of oxidoreductase activity":365,"response to muscle stretch":365,"APLYSIA CALIFORNICA":364,"Endoribonucleases producing 5'-phosphomonoesters.":364,"plasmodesma":364,"response to axon injury":364,"synapse assembly":364,"HslUV protease complex":363,"acetyl-CoA carboxylase activity":363,"-!- Formed by activation of proelastase from mammalian pancreas by trypsin. -!- Belongs to peptidase family S1. -!- Formerly EC 3.4.4.7 and EC 3.4.21.11.":362,"-!- May be identical to EC 1.8.1.10. -!- Formerly EC 1.6.4.5.":362,"DNA template":362,"Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.":362,"NADP--thioredoxin reductase. NADPH--thioredoxin reductase. NADPH:oxidized thioredoxin oxidoreductase. Thioredoxin reductase (NADPH).":362,"PERIPLASM":362,"Pancreatic elastase I. Pancreatopeptidase E.":362,"Pancreatic elastase.":362,"Proteasome subunit beta":362,"Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH.":362,"Thioredoxin-disulfide reductase.":362,"locomotory behavior":362,"2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL":361,"5'-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3'":361,"Aminopeptidase N":361,"RIBOSOMAL PROTEIN L14":361,"RIBOSOMAL PROTEIN L4":361,"Saccharomyces cerevisiae S288c":361,"TRANSCRIPTION REGULATION":361,"activation of GTPase activity":361,"antifungal humoral response":361,"env":361,"icosahedral virus, tombusviridae, RNA hairpin, virus coat protein, Swiss jelly roll fold, VIRUS-RNA complex":361,"mouse, human":361,"sulfate binding":361,"Chymotrypsin-like elastase family member 1":360,"Clostridium acetobutylicum ATCC 824":360,"Halobacterium salinarum NRC-1":360,"RIBOSOMAL PROTEIN L18":360,"S288C":360,"SIROHEME":360,"apolipoprotein binding":360,"regulation of cell size":360,"Complement Module, domain 1":359,"RIBOSOMAL PROTEIN L2":359,"RIBOSOMAL PROTEIN L5":359,"RIBOSOMAL PROTEIN L6":359,"positive regulation of wound healing":359,"-!- A group of multi-copper proteins of low specificity. -!- Acts on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. -!- The semiquinone may react further either enzymically or non- enzymically.":358,"4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.":358,"Ada2/Gcn5/Ada3 transcription activator complex":358,"CALIFORNIA SEA HARE":358,"Comamonas testosteroni":358,"Laccase.":358,"RIBOSOMAL PROTEIN L10E":358,"RIBOSOMAL PROTEIN L13":358,"RIBOSOMAL PROTEIN L15E":358,"RIBOSOMAL PROTEIN L18E":358,"RIBOSOMAL PROTEIN L21E":358,"RIBOSOMAL PROTEIN L23":358,"RIBOSOMAL PROTEIN L24E":358,"RIBOSOMAL PROTEIN L29":358,"RIBOSOMAL PROTEIN L30":358,"RIBOSOMAL PROTEIN L31E":358,"RIBOSOMAL PROTEIN L32E":358,"RIBOSOMAL PROTEIN L39E":358,"RIBOSOMAL PROTEIN L44E":358,"RIBOSOMAL PROTEIN L7AE":358,"Urishiol oxidase.":358,"positive regulation of miRNA metabolic process":358,"-!- Stereospecific for L-dopachrome (5,6-dioxo-2,3-5,6-tetrahydroindole- 2-carboxylate). -!- Dopachrome methyl ester is a substrate, but dopaminochrome (2,3- dihydroxyindolyl-5,6-quinone) is not (see also EC 4.1.1.84).":357,"A-site ASL SufA6":357,"ATP-dependent peptidase activity":357,"C21-steroid hormone biosynthetic process":357,"DCF. DCT. Dopachrome conversion factor. Dopachrome Delta(7),Delta(2)-isomerase. Dopachrome Delta-isomerase. Dopachrome isomerase. Dopachrome keto-enol isomerase. Dopachrome oxidoreductase. Dopachrome rearranging enzyme. Dopachrome tautomerase. L-dopachrome-methyl ester tautomerase. TRP. Tyrosinase-related protein 2.":357,"L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.":357,"L-dopachrome isomerase.":357,"RIBOSOMAL PROTEIN L10":357,"RIBOSOMAL PROTEIN L19E":357,"Rhodococcus jostii RHA1":357,"inositol phosphate metabolic process":357,"modulation of synaptic transmission":357,"positive regulation of ruffle assembly":357,"response to hyperoxia":357,"2-HYDROXYETHYL DISULFIDE":356,"Alanine racemase.":356,"GTP cyclohydrolase 1":356,"L-alanine = D-alanine.":356,"Myoglobin":356,"Shewanella oneidensis":356,"protein O-linked glycosylation":356,"sensory perception of pain":356,"-!- In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin. -!- Formerly EC 1.6.7.1 and EC 1.6.99.4.":355,"1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE":355,"2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH.":355,"Ferredoxin--NADP(+) reductase.":355,"HLA class II histocompatibility antigen, DRB1-1 beta chain":355,"Rhizobium etli CFN 42":355,"Serine/threonine-protein kinase pim-1":355,"endolysosome lumen":355,"positive regulation of cardioblast proliferation":355,"regulation of intracellular protein transport":355,"Mitogen-activated protein kinase 1":354,"microtubule cytoskeleton organization":354,"(2E,6E)-farnesyl diphosphate synthase.":353,"-!- Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. -!- The enzyme will not accept larger prenyl diphosphates as efficient donors.":353,"-!- The enzyme from Leishmania (both amastigote and promastigote forms) catalyzes the NADPH-dependent reduction of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. -!- It also catalyzes the reduction of 7,8-dihydropterins and 7,8- dihydrofolate to their tetrahydro forms. -!- In contrast to EC 1.5.1.3 and EC 1.5.1.34, pteridine reductase will not catalyze the reduction of the quinonoid form of dihydrobiopterin. -!- The enzyme is specific for NADPH; no activity has been detected with NADH. -!- It also differs from EC 1.5.1.3 in being specific for the B side of NADPH. -!- Formerly EC 1.1.1.253.":353,"5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 NADPH.":353,"CARBONMONOXIDE-(DICYANO) IRON":353,"Farnesyl pyrophosphate synthetase. Farnesyl-diphosphate synthase. FPP synthetase. Geranyltranstransferase.":353,"Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)- farnesyl diphosphate.":353,"HYDROSULFURIC ACID":353,"MR1":353,"Pteridine reductase 1. PTR1.":353,"Pteridine reductase.":353,"positive regulation of cellular component movement":353,"3',5'-cyclic-nucleotide phosphodiesterase activity":352,"Alpha-mannosidase 2":352,"Borrelia burgdorferi B31":352,"Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man(5)(GlcNAc)(3).":352,"ManII. Mannosidase II.":352,"Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase.":352,"RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN":352,"Rhodococcus":352,"encapsulation of foreign target":352,"ligase activity":352,"mRNA polyadenylation":352,"negative regulation of cell-cell adhesion":352,"protein localization to nucleus":352,"rhodopsin biosynthetic process":352,"NAD-dependent protein deacetylase activity":351,"Serine/threonine-protein kinase Chk1":351,"Urea + H(2)O = CO(2) + 2 NH(3).":351,"Urease.":351,"bacterial-type flagellum-dependent cell motility":351,"ciliary base":351,"kinase domain":351,"oxidative stress-induced premature senescence":351,"positive regulation of activated T cell proliferation":351,"potassium ion binding":351,"protein transporter activity":351,"selenium compound metabolic process":351,"tRNA acceptor end mimic":351,"transcriptional repressor activity, RNA polymerase II transcription factor binding":351,"ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.":350,"L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE":350,"Pantoate--beta-alanine ligase (AMP-forming).":350,"Pantoate-activating enzyme. Pantoic-activating enzyme. Pantothenate synthetase.":350,"Pantothenate synthetase":350,"antigen processing and presentation of exogenous peptide antigen via MHC class I":350,"calcium-mediated signaling using intracellular calcium source":350,"cytokine receptor binding":350,"heterotrimeric G-protein complex":350,"-!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3.":349,"-!- Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine.":349,"3-hydroxy-3-methylglutaryl-coenzyme A reductase":349,"5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine.":349,"CCA-adding enzyme":349,"Campylobacter pylori":349,"Dehydrolipoate dehydrogenase. Diaphorase. Dihydrolipoamide dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrothioctic dehydrogenase. E3 component of alpha-ketoacid dehydrogenase complexes. Glycine-cleavage system L-protein. L-protein. LDP-Glc. LDP-Val. Lipoamide dehydrogenase (NADH). Lipoamide oxidoreductase (NADH). Lipoamide reductase. Lipoamide reductase (NADH). Lipoate dehydrogenase. Lipoic acid dehydrogenase. Lipoyl dehydrogenase.":349,"Dihydrolipoyl dehydrogenase.":349,"Glycine hydroxymethyltransferase.":349,"Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.":349,"Ruegeria pomeroyi DSS-3":349,"Serine aldolase. Serine hydroxymethylase. Serine hydroxymethyltransferase. Threonine aldolase.":349,"UNDECYL-MALTOSIDE":349,"oligodendrocyte apoptotic process":349,"protein secretion":349,"urea cycle":349,"-!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, and EC 5.3.1.24).":348,"Anthranilate phosphoribosyltransferase.":348,"N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.":348,"N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide":348,"Phosphoribosyl-anthranilate diphosphorylase. Phosphoribosyl-anthranilate pyrophosphorylase.":348,"pteridine reductase activity":348,"wound healing, spreading of cells":348,"-!- Specific for 3',5'-cAMP and does not hydrolyze other nucleoside 3',5'-cyclic phosphates such as cGMP (cf. EC 3.1.4.17 and EC 3.1.4.35). -!- It is involved in modulation of the levels of cAMP, which is a mediator in the processes of cell transformation and proliferation. -!- Formerly EC 3.1.4.n1.":347,"3',5'-cyclic-AMP phosphodiesterase.":347,"Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate.":347,"Lys48-specific deubiquitinase activity":347,"P51":347,"Plasmodium vivax Sal-1":347,"VANADATE ION":347,"cAMP-specific PDE. cAMP-specific phosphodiesterase.":347,"phosphatidylinositol-4-phosphate binding":347,"2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.":346,"Bacillus phage phi29":346,"Carbamoyl-phosphate synthase large chain":346,"Lactoperoxidase.":346,"Peroxidase.":346,"Physeter catodon":346,"RECOMBINATION":346,"SPLICING":346,"antibiotic catabolic process":346,"mycolic acid biosynthetic process":346,"positive regulation of cell division":346,"HUPs":345,"HYDROLASE(O-GLYCOSYL)":345,"Prostaglandin G/H synthase 2":345,"Protein biosynthesis, ribosome, RNA, transfer, exit, peptidyl, 30S, 70S, 16S, ribosomal subunit, antibiotic, streptogramin":345,"Staphylococcus aureus subsp. aureus MW2":345,"cellular response to thyroid hormone stimulus":345,"costamere":345,"folic acid metabolic process":345,"histone H3-K4 methylation":345,"protein export from nucleus":345,"Candida albicans SC5314":344,"P66":344,"acetylglucosaminyltransferase activity":344,"calcium ion transmembrane transport":344,"embryo development ending in birth or egg hatching":344,"methotrexate binding":344,"mitogen-activated protein kinase binding":344,"negative regulation of cell aging":344,"BH3 domain binding":343,"CELL INVASION":343,"Corynebacterium":343,"DIHYDROFLAVINE-ADENINE DINUCLEOTIDE":343,"Mesorhizobium loti":343,"Neisseria gonorrhoeae":343,"O-SIALIC ACID":343,"Viomycin":343,"galactose binding":343,"lamellipodium membrane":343,"regulation of ryanodine-sensitive calcium-release channel activity":343,"signal transduction by p53 class mediator":343,"transcription factor activity, core RNA polymerase binding":343,"viral budding from plasma membrane":343,"Anopheles gambiae":342,"EXTRACELLULAR DOMAIN":342,"Enterovirus A71":342,"Glutathione S-transferase P":342,"UNKNOWN PROTEIN M2":342,"UNKNOWN PROTEIN P1":342,"UNKNOWN PROTEIN P2":342,"Xanthomonas campestris pv. campestris":342,"cellular response to fluid shear stress":342,"mitotic spindle checkpoint":342,"positive regulation of autophagy":342,"CYSTEINE":341,"Corynebacterium diphtheriae":341,"ESR1, ESR, NR3A1":341,"GLUTAMINE":341,"L-phenylalanine biosynthetic process":341,"LEUCINE":341,"NAD biosynthesis via nicotinamide riboside salvage pathway":341,"RNA phosphodiester bond hydrolysis, exonucleolytic":341,"acetyl-CoA biosynthetic process":341,"carbamoyl-phosphate synthase (ammonia) activity":341,"lactation":341,"negative regulation of blood vessel endothelial cell migration":341,"negative regulation of low-density lipoprotein particle receptor biosynthetic process":341,"replication fork processing":341,"-!- The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4.":340,"ATCC 700084 / mc(2)155":340,"Adenosylhomocysteinase.":340,"Adenosylhomocysteine hydrolase. AdoHcyase. S-adenosylhomocysteinase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine synthase. SAHase.":340,"BETA-D-GLUCOSE":340,"DNA replication-independent nucleosome assembly":340,"Lactococcus lactis":340,"RNA-DIRECTED RNA POLYMERASE":340,"S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine.":340,"alpha-catenin binding":340,"dopamine catabolic process":340,"positive regulation of viral transcription":340,"potassium channel inhibitor activity":340,"regulation of lamellipodium assembly":340,"ACETYLCHOLINESTERASE":339,"Cell division protein kinase 2":339,"Fibroblast growth factor 1":339,"In phosphorus-containing anhydrides.":339,"Tyrosine-protein kinase ABL1":339,"core promoter proximal region sequence-specific DNA binding":339,"positive regulation of interferon-gamma biosynthetic process":339,"Aspergillus oryzae RIB40":338,"Enoylpyruvate transferase. MurA transferase. Phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase. Phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase. Pyruvate-UDP-acetylglucosamine transferase. Pyruvate-uridine diphospho-N-acetyl-glucosamine transferase. Pyruvate-uridine diphospho-N-acetylglucosamine transferase. Pyruvic-uridine diphospho-N-acetylglucosaminyltransferase. UDP-N-acetylglucosamine 1-carboxyvinyl-transferase. UDP-N-acetylglucosamine enoylpyruvyltransferase.":338,"GALLUS GALLUS":338,"HTA426":338,"Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP- N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.":338,"UDP-N-acetylglucosamine 1-carboxyvinyltransferase.":338,"host cell membrane":338,"mesoderm formation":338,"pathway-restricted SMAD protein phosphorylation":338,"pyrimidine nucleobase biosynthetic process":338,"response to pH":338,"response to water deprivation":338,"suppression by virus of host translation":338,"-!- This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. -!- The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). -!- Belongs to peptidase family M24A.":337,"ADENOSINE-5-DIPHOSPHORIBOSE":337,"CACODYLIC ACID":337,"CHICKEN":337,"Deinococcus":337,"Methionine aminopeptidase. Peptidase M.":337,"Methionyl aminopeptidase.":337,"Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.":337,"S-nitrosoglutathione binding":337,"dinitrosyl-iron complex binding":337,"heme biosynthetic process":337,"pyruvate dehydrogenase complex":337,"-!- This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli. -!- Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli. -!- The enzyme has weak peptidase activity with casein and other non- native substrates. -!- The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. -!- Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding. -!- They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding. -!- If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme. -!- Belongs to peptidase family S1B.":336,"ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate.":336,"ATP:pantothenate 4'-phosphotransferase. D-pantothenate kinase. Pantothenate kinase (phosphorylating). Pantothenic acid kinase.":336,"Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.":336,"High temperature requirement protease A. HrtA heat shock protein. Protease Do.":336,"PIK3CG":336,"Pantothenate kinase.":336,"Peptidase Do.":336,"S-adenosylmethionine metabolic process":336,"Transferase/Transferase inhibitor":336,"cellular copper ion homeostasis":336,"complement component C1q binding":336,"methyltransferase activity":336,"retina development in camera-type eye":336,"GTPase activating protein binding":335,"L-phenylalanine biosynthetic process from chorismate via phenylpyruvate":335,"Lactobacillus casei":335,"Tubulin alpha chain":335,"UNP residues 25-300":335,"bile acid binding":335,"integrin alphav-beta3 complex":335,"negative regulation of lipoprotein metabolic process":335,"negative regulation of serine-type endopeptidase activity":335,"regulation of endothelial tube morphogenesis":335,"toll-like receptor 9 signaling pathway":335,"DNA (5'-D(P*GP*TP*CP*GP*G)-3')":334,"HCV":334,"O157:H7":334,"Protocatechuate 3,4-dioxygenase alpha chain":334,"SUGAR (10-MER)":334,"histone methyltransferase complex":334,"mRNA cap binding complex":334,"Alcaligenes":333,"MOUSE-EAR CRESS":333,"MRSA252":333,"Protocatechuate 3,4-dioxygenase beta chain":333,"RNA uridylyltransferase activity":333,"Serine/threonine-protein kinase B-raf":333,"dopachrome isomerase activity":333,"heart morphogenesis":333,"phenylpyruvate tautomerase activity":333,"polysaccharide assembly with MHC class II protein complex":333,"regulation of circadian rhythm":333,"tau-protein kinase activity":333,"ASPARTATE AMINOTRANSFERASE":332,"CYCLIN A2":332,"D-alanine--D-alanine ligase":332,"Enterobacter cloacae":332,"Fumarate reductase flavoprotein subunit":332,"MYCOBACTERIUM SMEGMATIS":332,"OXALOACETATE ION":332,"Rhodococcus sp.":332,"histone H3-K36 demethylation":332,"positive regulation of p38MAPK cascade":332,"regulation of cyclin-dependent protein serine/threonine kinase activity":332,"tetrahydrobiopterin biosynthetic process":332,"zymogen activation":332,"-!- The enzyme catalyzes the interconversion of aldose and ketose sugars with broad substrate specificity. -!- The enzyme binds the closed form of its sugar substrate (in the case of glucose, only the alpha anomer) and catalyzes ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. -!- Isomerization proceeds via a hydride-shift mechanism.":331,"Arthrobacter":331,"Bacteroides ovatus ATCC 8483":331,"D-xylopyranose = D-xylulose.":331,"D-xylose ketoisomerase.":331,"OXIDOREDUCTASE/ELECTRON TRANSPORT":331,"Shewanella":331,"T-cell surface glycoprotein CD4":331,"Xylose isomerase":331,"Xylose isomerase.":331,"glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity":331,"positive regulation of protein import into nucleus, translocation":331,"protein localization to cell surface":331,"-!- Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria. -!- Also provides the malonyl groups for polyketide biosynthesis. -!- The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. -!- In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate. -!- This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89. -!- Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase. -!- In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates. -!- The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.":330,"Acyl carrier protein malonyltransferase. Malonyl coenzyme A-acyl carrier protein transacylase. Malonyl transacylase. Malonyl transferase. Malonyl-CoA-acyl carrier protein transacylase. Malonyl-CoA/dephospho-CoA acyltransferase. MCAT.":330,"Aspergillus nidulans FGSC A4":330,"Calmodulin":330,"Francisella tularensis subsp. tularensis":330,"Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein].":330,"RNA catabolic process":330,"[Acyl-carrier-protein] S-malonyltransferase.":330,"activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway":330,"dendrite morphogenesis":330,"poly(A)+ mRNA export from nucleus":330,"positive regulation of transcription regulatory region DNA binding":330,"release of cytochrome c from mitochondria":330,"response to mechanical stimulus":330,"-!- The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis. -!- The mechanism has been shown to be a retroaldol/aldol reaction.":329,"-!- The substrate is the quinonoid form of dihydropteridine. -!- Not identical with EC 1.5.1.3. -!- Formerly EC 1.6.99.7 and EC 1.6.99.10.":329,"1-deoxy-D-xylulose-5-phosphate reductoisomerase.":329,"1-deoxyxylulose-5-phosphate reductoisomerase. DXP-reductoisomerase.":329,"2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + NADPH.":329,"6,7-dihydropteridine reductase.":329,"6,7-dihydropteridine:NAD(P)H oxidoreductase. DHPR. Dihydropteridine (reduced nicotinamide adenine dinucleotide) reductase. Dihydropteridine reductase. Dihydropteridine reductase (NADH). NAD(P)H(2):6,7-dihydropteridine oxidoreductase. NADH-dihydropteridine reductase. NADPH-dihydropteridine reductase. NADPH-specific dihydropteridine reductase.":329,"A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H.":329,"ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl- tRNA(Trp).":329,"DSM 2661":329,"L-tryptophan-tRNA(Trp) ligase (AMP-forming). TrpRS. Tryptophan translase. Tryptophanyl ribonucleic synthetase. Tryptophanyl-transfer ribonucleate synthetase. Tryptophanyl-transfer ribonucleic acid synthetase. Tryptophanyl-transfer ribonucleic synthetase. Tryptophanyl-transfer RNA synthetase. Tryptophanyl-tRNA synthase. Tryptophanyl-tRNA synthetase.":329,"Listeria innocua Clip11262":329,"MYOGLOBIN":329,"S-adenosylmethionine-dependent methyltransferase activity":329,"Tryptophan--tRNA ligase.":329,"fructose metabolic process":329,"protein-lysine N-methyltransferase activity":329,"small GTPase mediated signal transduction":329,"thiol-dependent ubiquitinyl hydrolase activity":329,"Cavia porcellus":328,"JM109":328,"estrogen metabolic process":328,"negative regulation of tumor necrosis factor-mediated signaling pathway":328,"positive regulation of interleukin-2 biosynthetic process":328,"transforming growth factor beta binding":328,"Chromobacterium violaceum ATCC 12472":327,"Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl- protein + diphosphate.":327,"HIV-1 PROTEASE":327,"HYDROLASE/IMMUNE SYSTEM":327,"Jellyfish":327,"N-OXALYLGLYCINE":327,"SRC":327,"STREPTOMYCES COELICOLOR":327,"Viral Protein":327,"heterochromatin":327,"negative regulation of PERK-mediated unfolded protein response":327,"positive regulation of protein kinase A signaling":327,"transcription cofactor activity":327,"5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE":326,"Adenosylhomocysteinase":326,"Anthranilate phosphoribosyltransferase":326,"Cytochrome c1, heme protein, mitochondrial":326,"RAGE receptor binding":326,"Structural Genomics, Unknown function":326,"URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE":326,"histone demethylase activity (H3-K36 specific)":326,"immunoglobulin mediated immune response":326,"positive regulation of substrate-dependent cell migration, cell attachment to substrate":326,"-!- Formerly EC 4.1.2.16.":325,"2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating). 2-dehydro-3-deoxy-phosphooctonate aldolase. 2-keto-3-deoxy-8-phosphooctonic synthetase. 3-deoxy-D-manno-octulosonate-8-phosphate synthase. 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase. 3-deoxy-D-mannooctulosonate-8-phosphate synthetase. 3-deoxyoctulosonic 8-phosphate synthetase. KDO-8-P synthase. KDO-8-phosphate synthetase. KDOP synthase. Phospho-2-keto-3-deoxyoctonate aldolase.":325,"2-oxoglutarate metabolic process":325,"3-deoxy-8-phosphooctulonate synthase.":325,"Ascaris suum":325,"PLASMODIUM FALCIPARUM":325,"Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 3-deoxy-D-manno- octulosonate 8-phosphate + phosphate.":325,"Synechococcus":325,"Transferase(Phosphotransferase) domain 1":325,"UDP-glucose metabolic process":325,"fission yeast":325,"negative regulation of hydrogen peroxide-induced cell death":325,"negative regulation of protein serine/threonine kinase activity":325,"positive regulation of translational initiation":325,"regulation of epithelial cell migration":325,"steroid biosynthetic process":325,"strand displacement":325,"-!- Belongs to peptidase family M10B.":324,"-!- Most of the bacterial and archaeal enzymes consist of only an oxidase domain and function together with bacterial ferredoxins. -!- The enzyme from the delta-proteobacterium Sorangium cellulosum also includes a reductase domain that binds FAD, FMN and a [2Fe-2S] cluster. -!- The similar enzymes from plants and animals use only NADPH as acceptor (cf. EC 1.14.13.39).":324,"2 L-arginine + 3 NAD(P)H + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NAD(P)(+) + 4 H(2)O.":324,"Bacillus licheniformis":324,"Lactobacillus plantarum":324,"N-OCTANE":324,"Nitric oxide synthase oxygenase":324,"Nitric oxide synthetase. NO synthase.":324,"Nitric-oxide synthase (NAD(P)H).":324,"RNA, ribosome, tRNA, translation, mRNA":324,"T-cell receptor beta-1 chain C region":324,"glycosaminoglycan biosynthetic process":324,"negative regulation of osteoclast development":324,"protein kinase A regulatory subunit binding":324,"regulation of stress fiber assembly":324,"response to reactive oxygen species":324,"response to unfolded protein":324,"-!- This enzyme completes each cycle of fatty acid elongation by catalyzing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl- carrier protein. -!- It is one of the activities of EC 2.3.1.85. -!- The mammalian enzyme is Re-specific with respect to NADP(+) (cf. EC 1.3.1.10 and and EC 1.3.1.104).":323,"Acyl-ACP dehydrogenase. Enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific).":323,"Cryptosporidium parvum":323,"Enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific).":323,"Gag polyprotein":323,"Glutathione S-transferase":323,"MOLYBDENUM(IV) ION":323,"RIBOSOMAL PROTEIN L37Ae":323,"RNA, ribosome, tRNA, translation, mRNA, RIBOSOME-ANTIBIOTIC complex":323,"UDP-N-acetylglucosamine 1-carboxyvinyltransferase":323,"negative regulation of stress fiber assembly":323,"positive regulation of leukocyte chemotaxis":323,"-!- Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). -!- These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which leads to the apoptotic phenotype. -!- Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B. -!- Caspase-3 can activate procaspase-2 (EC 3.4.22.55). -!- Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain. -!- While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate. -!- Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|- is a better substrate than Asp-Val-Ala-Asp-|-. -!- This is not the case for caspase-7. -!- Belongs to peptidase family C14.":322,"-!- Formerly EC 2.4.2.13.":322,"A3(2)":322,"ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine.":322,"AdoMet synthetase. S-adenosylmethionine synthetase.":322,"Apopain. CASP-3. CPP32. Yama protein.":322,"Caspase-3":322,"Caspase-3.":322,"Methionine adenosyltransferase.":322,"PA01":322,"Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.":322,"TRANSFERASE/ANTIBIOTIC":322,"Vaccinia virus":322,"chromosome, telomeric region":322,"oxidative demethylation":322,"positive regulation of ubiquitin protein ligase activity":322,"DNA ligation":321,"HEPTANE-1,2,3-TRIOL":321,"Methylamine dehydrogenase light chain":321,"Plasmodium vivax":321,"Sulfolobus acidocaldarius DSM 639":321,"carboxylic acid metabolic process":321,"cellular response to glucose stimulus":321,"signal transducer activity, downstream of receptor":321,"KIRROMYCIN":320,"SCF ubiquitin ligase complex":320,"azurophil granule membrane":320,"fermentation":320,"regulation of tumor necrosis factor production":320,"-!- Wide specificity for 5'-nucleotides.":319,"5'-nucleotidase.":319,"A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.":319,"ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440":319,"Aspartate carbamoyltransferase catalytic subunit":319,"BIOTIN-BINDING PROTEIN":319,"Bovine":319,"DIUNDECYL PHOSPHATIDYL CHOLINE":319,"Lactobacillus plantarum WCFS1":319,"Pyruvate kinase":319,"antigen processing and presentation of peptide or polysaccharide antigen via MHC class II":319,"cellular amino acid metabolic process":319,"cellular response to magnesium ion":319,"centrosome cycle":319,"clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane":319,"ligase":319,"light chain":319,"quinone binding":319,"smooth muscle cell migration":319,"stem cell population maintenance":319,"suppression by virus of host ISG15 activity":319,"ACETYL GROUP":318,"TTR, PALB":318,"histone H3-K4 trimethylation":318,"mRNA (nucleoside-2'-O-)-methyltransferase activity":318,"mRNA methylation":318,"tube formation":318,"BACE, BACE1, KIAA1149":317,"FK506 binding":317,"FUSIDIC ACID":317,"GTPase HRas":317,"Rhizobium etli":317,"S,R MESO-TARTARIC ACID":317,"branch elongation involved in ureteric bud branching":317,"cornification":317,"dipeptidase activity":317,"hypothetical protein":317,"mesonephric epithelium development":317,"negative regulation of endothelial cell proliferation":317,"negative regulation of interferon-gamma production":317,"positive regulation of fever generation":317,"regulation of cytokinesis":317,"transferrin transport":317,"BL21(DE3)":316,"EXTRACELLULAR":316,"SERINE":316,"metalloexopeptidase activity":316,"positive regulation of tumor necrosis factor-mediated signaling pathway":316,"somatic stem cell population maintenance":316,"viral protein processing":316,"Alanine racemase":315,"IDE":315,"Methylamine dehydrogenase heavy chain":315,"Ribulose bisphosphate carboxylase":315,"Schizosaccharomyces":315,"activin binding":315,"artificial gene":315,"glutamate biosynthetic process":315,"negative regulation of Rho protein signal transduction":315,"positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway":315,"-!- The enzyme also reduces nitric oxide and hydroxylamine to ammonia, and sulfite to sulfide.":314,"ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe).":314,"Aspergillus fumigatus":314,"Cytochrome c nitrite reductase. Cytochrome c552. Multiheme nitrite reductase.":314,"DSM 4304":314,"NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+).":314,"Nitrite reductase (cytochrome; ammonia-forming).":314,"Phenylalanine translase. Phenylalanyl-tRNA synthetase.":314,"Phenylalanine--tRNA ligase.":314,"SH3 Domains":314,"SPHEROIDENE":314,"cGMP-stimulated cyclic-nucleotide phosphodiesterase activity":314,"cytoplasmic side of endoplasmic reticulum membrane":314,"embryonic digit morphogenesis":314,"modulation by virus of host protein ubiquitination":314,"negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress":314,"positive regulation of chemokine production":314,"positive regulation of ubiquitin-specific protease activity":314,"purine nucleotide catabolic process":314,"voltage-gated cation channel activity":314,"DPP4, ADCP2, CD26":313,"NCTC 11168":313,"Peptidyl-prolyl cis-trans isomerase A":313,"TRANSFERASE, HYDROLASE":313,"acetylcholine catabolic process":313,"acetylcholinesterase activity":313,"beta-catenin destruction complex assembly":313,"polydeoxyribonucleotide/polyribonucleotide hybrid":313,"Coagulation factor VII":312,"UBC":312,"aromatase activity":312,"b1732, JW1721, katE":312,"basement membrane":312,"endodeoxyribonuclease activity":312,"phospholipase binding":312,"positive regulation of cellular protein metabolic process":312,"protein transport":312,"regulation of glycolytic process":312,"response to amine":312,"-!- Formerly EC 4.2.1.52.":311,"-!- Wide specificity. -!- Formerly EC 1.1.1.139.":311,"1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE":311,"4-hydroxy-tetrahydrodipicolinate synthase.":311,"45-meric":311,"Alditol + NAD(P)(+) = aldose + NAD(P)H.":311,"Aldose reductase. Polyol dehydrogenase (NADP(+)).":311,"Asparaginase.":311,"DHDPS. Dihydrodipicolinate synthetase.":311,"L-asparaginase. L-asparagine amidohydrolase.":311,"L-asparagine + H(2)O = L-aspartate + NH(3).":311,"Methanococcus jannaschii":311,"Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5- tetrahydro-(2S)-dipicolinate + H(2)O.":311,"THYMIDINE-5'-DIPHOSPHATE":311,"Vibrio cholerae O1 biovar El Tor":311,"melanosome":311,"regulation of Rac protein signal transduction":311,"response to copper ion":311,"tryptophan catabolic process":311,"-!- Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis.":310,"3-oxosteroid isomerase. Delta(5)-3-keto steroid isomerase. Delta(5)-3-ketosteroid isomerase. Delta(5)-3-oxosteroid isomerase. Delta(5)-steroid isomerase. Hydroxysteroid isomerase. Steroid isomerase.":310,"A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid.":310,"ARCHAEOGLOBUS FULGIDUS":310,"Cytochrome c oxidase polypeptide VIc":310,"Cytochrome c oxidase subunit 5A":310,"Cytochrome c oxidase subunit 5B":310,"Cytochrome c oxidase subunit 7C":310,"Steroid Delta-isomerase.":310,"clathrin binding":310,"hydrolase activity, acting on ester bonds":310,"modulation by virus of host autophagy":310,"monocyte chemotaxis":310,"myosin II binding":310,"positive regulation of transcription from RNA polymerase III promoter":310,"stress fiber assembly":310,"transcription, RNA-templated":310,"-!- NAD(+) cannot replace NADP(+). -!- In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10.":309,"5-dehydroshikimate reductase. 5-dehydroshikimic reductase. Dehydroshikimic reductase. DHS reductase. Shikimate 5-dehydrogenase. Shikimate oxidoreductase. Shikimate:NADP(+) 5-oxidoreductase. Shikimate:NADP(+) oxidoreductase.":309,"INTEGRASE":309,"Shikimate + NADP(+) = 3-dehydroshikimate + NADPH.":309,"Shikimate dehydrogenase.":309,"fructose biosynthetic process":309,"macrophage chemotaxis":309,"negative regulation of glycogen biosynthetic process":309,"positive regulation of interleukin-10 production":309,"translation initiation factor activity":309,"-!- Cyclomaltodextrins (Schardinger dextrins) of various sizes (6, 7, 8, etc. glucose units) are formed reversibly from starch and similar substrates. -!- Also disproportionates linear maltodextrins without cyclizing (cf. EC 2.4.1.25).":308,"-!- The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor. -!- The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant toward other amine acceptors, such as spermidine and cadaverine. -!- Cf. EC 2.5.1.22 and EC 2.5.1.23.":308,"14-3-3 protein binding":308,"927/4 GUTat10.1":308,"Aminopropyltransferase. Putrescine aminopropyltransferase.":308,"Bacillus macerans amylase. Cyclodextrin glucanotransferase. Cyclodextrin glycosyltransferase.":308,"Chlorobium tepidum TLS":308,"Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)- alpha-D-glucosidic bond.":308,"Cyclomaltodextrin glucanotransferase":308,"Cyclomaltodextrin glucanotransferase.":308,"ENDOCYTOSIS":308,"Inorganic pyrophosphatase":308,"Plasmodium falciparum FcB1/Columbia":308,"S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl- 5'-thioadenosine + spermidine.":308,"Spermidine synthase.":308,"histone deacetylase complex":308,"misfolded or incompletely synthesized protein catabolic process":308,"phospholipid metabolic process":308,"positive regulation of apoptotic process in other organism":308,"regulation of hepatocyte growth factor receptor signaling pathway":308,"-!- Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). -!- Methylene blue and other acceptors can also be reduced.":307,"Cytochrome c3 reductase. Cytochrome hydrogenase. H(2):ferricytochrome c3 oxidoreductase.":307,"Cytochrome-c3 hydrogenase.":307,"H(2) + 2 ferricytochrome c3 = 2 H(+) + 2 ferrocytochrome c3.":307,"Methanothermobacter marburgensis str. Marburg":307,"histone H2A monoubiquitination":307,"integrin activation":307,"negative regulation of circadian rhythm":307,"oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor":307,"Aspartate-semialdehyde dehydrogenase":306,"Human spumaretrovirus":306,"TTL":306,"Tyrosine-protein phosphatase non-receptor type 1":306,"cellular response to non-ionic osmotic stress":306,"cellular response to steroid hormone stimulus":306,"cellular response to unfolded protein":306,"positive regulation of prostaglandin biosynthetic process":306,"positive regulation of receptor catabolic process":306,"pyrimidine nucleoside salvage":306,"sigma factor antagonist activity":306,"vascular endothelial growth factor-activated receptor activity":306,"-!- Brings about the conversion of one topological isomer of DNA into another, e.g. the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences (cf. EC 5.99.1.3).":305,"-!- Involved in the biosynthesis of vitamin K(2) (menaquinone). -!- In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. -!- It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO(2) but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20. -!- Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC. -!- Formerly EC 2.5.1.64 and EC 2.5.1.n1.":305,"2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase":305,"2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase.":305,"ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.":305,"CO92":305,"DEINOCOCCUS RADIODURANS":305,"DIGALACTOSYL DIACYL GLYCEROL (DGDG)":305,"DNA topoisomerase I. Nicking-closing enzyme. Omega-protein. Relaxing enzyme. Swivelase. Type I DNA topoisomerase. Untwisting enzyme.":305,"DNA topoisomerase.":305,"Dihydroorotate dehydrogenase (fumarate)":305,"Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl- cyclohex-3-ene-1-carboxylate + CO(2).":305,"PHOSPHATIDYLETHANOLAMINE":305,"Peptide deformylase":305,"Phi29-like viruses":305,"SEPHCHC synthase.":305,"SUGAR (NAG-NAG)":305,"Small nuclear ribonucleoprotein F":305,"acrB, acrE, b0462, JW0451":305,"cAMP-dependent protein kinase complex":305,"calcium-dependent cysteine-type endopeptidase activity":305,"negative regulation of JAK-STAT cascade":305,"peptide metabolic process":305,"tRNA":305,"2-dehydro-3-deoxyphosphooctonate aldolase":304,"Achromobacter xylosoxidans":304,"Amine oxidase [flavin-containing] B":304,"Benzoylformate = benzaldehyde + CO(2).":304,"Benzoylformate carboxy-lyase.":304,"Benzoylformate decarboxylase":304,"Benzoylformate decarboxylase.":304,"UNKNOWN PROTEIN CHAIN M2":304,"UNKNOWN PROTEIN CHAIN P1":304,"UNKNOWN PROTEIN CHAIN P2":304,"Uracil-DNA glycosylase":304,"chromatin silencing at telomere":304,"homophilic cell adhesion via plasma membrane adhesion molecules":304,"innate immune response in mucosa":304,"response to cholesterol":304,"histone H3-K4 demethylation":303,"rpoD, alt, b3067, JW3039":303,"630":302,"CHLAMYDOMONAS REINHARDTII":302,"Ralstonia eutropha":302,"insulin-like growth factor receptor binding":302,"negative regulation of T cell proliferation":302,"positive regulation of interleukin-12 production":302,"regulation of phagocytosis":302,"C2- domain Calcium/lipid binding domain":301,"NITRIC OXIDE SYNTHASE, ENDOTHELIAL":301,"arginine biosynthetic process":301,"extrinsic apoptotic signaling pathway via death domain receptors":301,"low-density lipoprotein particle clearance":301,"negative regulation of endopeptidase activity":301,"nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay":301,"protein unfolding":301,"regulation of heart rate":301,"vacuole":301,"-!- Will not accept larger prenyl diphosphates as efficient donors.":300,"Acting on acid anhydrides; catalyzing transmembrane movement of substances.":300,"Bacillus megaterium NBRC 15308 = ATCC 14581":300,"Bifunctional cytochrome P450/NADPH--P450 reductase":300,"Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.":300,"Dimethylallyltransferase. Geranyl-diphosphate synthase. Prenyltransferase.":300,"Dimethylallyltranstransferase.":300,"ISOMERASE/ISOMERASE INHIBITOR":300,"OXIDOREDUCTASE, INHIBITOR COMPLEX":300,"RIBOSOMAL PROTEIN S6":300,"SARS-CoV":300,"maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter":300,"memory":300,"regulation of translation":300,"sarcomere organization":300,"(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)- diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala- gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.":299,"-!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. -!- Involved in the synthesis of cell-wall peptidoglycan.":299,"Bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)- pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D- glucosaminyltransferase. Penicillin binding protein (3 or 1B). Peptidoglycan TGase. Peptidoglycan transglycosylase. PG-II.":299,"Clostridium perfringens ATCC 13124":299,"GTP cyclohydrolase I activity":299,"Peptidoglycan glycosyltransferase.":299,"Phenylethylamine oxidase":299,"Tail spike protein":299,"Von Hippel-Lindau disease tumor suppressor":299,"mouse-ear cress":299,"peptidyl-lysine deacetylation":299,"positive regulation of calcium ion import":299,"protein N-acetylglucosaminyltransferase activity":299,"regulation of glucose metabolic process":299,"Aldose reductase":298,"Bordetella pertussis Tohama I":298,"Clostridium acetobutylicum":298,"GLUTATHIONE S-TRANSFERASE":298,"Prp19 complex":298,"SINEFUNGIN":298,"detection of bacterium":298,"nicotinate-nucleotide adenylyltransferase activity":298,"protein K63-linked ubiquitination":298,"protein catabolic process":298,"-!- Brings about the opening of the epidioxy bridge.":297,"-!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzyme A group is subsequently removed from the product by EC 3.1.2.28.":297,"1,4-dihydroxy-2-naphthoyl-CoA synthase":297,"1,4-dihydroxy-2-naphthoyl-CoA synthase.":297,"4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O.":297,"DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing).":297,"Pro-Pol polyprotein":297,"RIBOSOMAL PROTEIN S8":297,"cellular response to interferon-beta":297,"heavy chain":297,"nuclear envelope organization":297,"nuclear hormone receptor binding":297,"podosome":297,"Acidic ribosomal protein P0 homolog":296,"C-TERMINAL DOMAIN":296,"ENDOCYTOSIS/EXOCYTOSIS":296,"Novosphingobium aromaticivorans DSM 12444":296,"Pyrococcus abyssi":296,"antibiotic biosynthetic process":296,"cell septum":296,"diphthine synthase":296,"host cell perinuclear region of cytoplasm":296,"polysaccharide binding":296,"protein-arginine N-methyltransferase activity":296,"purine-nucleoside phosphorylase activity":296,"(1) L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. (2) L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate. (3) L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.":295,"-!- Also acts on L-isoleucine and L-valine. -!- Different from EC 2.6.1.66.":295,"Branched-chain amino acid aminotransferase. Transaminase B.":295,"Branched-chain-amino-acid transaminase.":295,"Calmodulin-sensitive adenylate cyclase":295,"Neurospora crassa OR74A":295,"PYROPHOSPHATE":295,"bicellular tight junction assembly":295,"death-inducing signaling complex assembly":295,"leukocyte tethering or rolling":295,"ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).":294,"Acting on amino acids and derivatives.":294,"Camphor 5-monooxygenase":294,"Coxiella burnetii":294,"Endo-1,4-beta-xylanase":294,"Glutamate--tRNA ligase.":294,"Glutamic acid translase. Glutamyl-tRNA synthetase.":294,"HEME DOMAIN, RESIDUES 297-718":294,"ISOPROPYL-1-BETA-D-THIOGALACTOSIDE":294,"Leishmania":294,"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1":294,"mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)":294,"photoreceptor disc membrane":294,"5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL":293,"ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL":293,"ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL":293,"DNA template strand":293,"Glycogen Phosphorylase B;":293,"Ion transport protein":293,"Mo-molybdopterin cofactor biosynthetic process":293,"Mouse-ear cress":293,"RIBOSOMAL PROTEIN S7":293,"RNA polymerase sigma factor rpoD":293,"Salmonella enterica":293,"T cell receptor complex":293,"cerebral cortex development":293,"chloroplast thylakoid membrane":293,"chromatin assembly or disassembly":293,"mtrB":293,"peripheral nervous system development":293,"succinate dehydrogenase activity":293,"viral RNA genome replication":293,"(R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH.":292,"-!- Catalyzes the insertion of molybdenum into the ene-dithiol group of molybdopterin. -!- In eukaryotes this reaction is catalyzed by the N-terminal domain of a fusion protein whose C-terminal domain catalyzes EC 2.7.7.75.":292,"-!- The enzyme is inactivated by EC 2.7.11.31 and reactivated by EC 3.1.3.47.":292,"-!- Wide specificity. -!- Also catalyzes transphosphorylations.":292,"3-hydroxy-3-methylglutaryl-coenzyme A reductase. HMG-CoA reductase.":292,"ATP synthase subunit delta":292,"Acid phosphatase.":292,"Acid phosphomonoesterase. Glycerophosphatase. Phosphomonoesterase.":292,"Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.":292,"Aspartate Aminotransferase, domain 1":292,"Extracellular domain":292,"Hydroxymethylglutaryl-CoA reductase (NADPH).":292,"Influenza A virus (A/Viet Nam/1203/2004(H5N1))":292,"MRF binding":292,"Molybdopterin molybdotransferase.":292,"Oxidoreductase/Oxidoreductase inhibitor":292,"hydroxymethylglutaryl-CoA reductase activity":292,"lipid particle organization":292,"positive regulation of mitochondrial fission":292,"POLH, RAD30, RAD30A, XPV":291,"dATP catabolic process":291,"growth factor receptor binding":291,"negative regulation of epithelial cell proliferation":291,"-!- ITP can act as phosphate donor.":290,"Altronate hydrolase. D-mannonate hydro-lyase. Mannonic hydrolase.":290,"Cancer, Proteasome, Bortezomib, Drug Resistance, Binding Analysis, HYDROLASE":290,"D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H(2)O.":290,"GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2).":290,"HYDROLASE/HYDROLASE ACTIVATOR":290,"Mannonate dehydratase.":290,"Metallo-beta-lactamase type 2":290,"Phosphoenolpyruvate carboxykinase (GTP).":290,"Porphyromonas gingivalis W83":290,"RIBOSOMAL PROTEIN S5":290,"Ricinus communis":290,"[Pseudomonas syringae] pv. tomato str. DC3000":290,"bone morphogenesis":290,"calcium channel activity":290,"host cell endoplasmic reticulum":290,"miRNA binding":290,"phosphate ion binding":290,"positive regulation of histone H3-K27 methylation":290,"positive regulation of immune response":290,"protein autoprocessing":290,"regulation of viral genome replication":290,"signal complex assembly":290,"-!- Hydrolyzes alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu and folylpoly-gamma- glutamates. -!- With folylpoly-gamma-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate. -!- Does not hydrolyze Ac-beta-Asp-Glu. -!- Inhibited by quisqualic acid, Ac-beta-Asp-Glu, and 2-phosphonomethyl- pentanedioate. -!- The release of C-terminal glutamate from folylpoly-gamma-glutamates is also catalyzed by EC 3.4.17.11 and EC 3.4.19.9. -!- Belongs to peptidase family M28. -!- Formerly EC 3.4.19.8.":289,"5'-D(P*GP*TP*CP*GP*G)-3'":289,"Bacteriorhodopsin":289,"Farnesyl pyrophosphate synthase":289,"Folate hydrolase. N-acetylated-gamma-linked-acidic dipeptidase. NAALADase. Pteroylpoly-gamma-glutamate carboxypeptidase.":289,"Glutamate carboxypeptidase II.":289,"Mandelate racemase/muconate lactonizing enzyme":289,"Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.":289,"Transferring phosphorus-containing groups.":289,"positive regulation of endothelial cell chemotaxis":289,"protein kinase A signaling":289,"F2":288,"R6":288,"RIBOSOMAL PROTEIN S15":288,"RIBOSOMAL PROTEIN S17":288,"UDP-glucose 6-dehydrogenase":288,"alphav-beta3 integrin-vitronectin complex":288,"negative regulation of protein autophosphorylation":288,"positive regulation of lamellipodium assembly":288,"positive thymic T cell selection":288,"synapse organization":288,"trypsinogen activation":288,"(1) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine. (2) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-glucosamine.":287,"-!- Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. -!- EC 2.4.1.155 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.":287,"Burkholderia":287,"DNA polymerase I, thermostable":287,"Glycoside hydrolase O-GlcNAcase. O-GlcNAc hydrolase. O-GlcNAcase. OGA.":287,"JUN kinase activity":287,"Protein O-GlcNAcase.":287,"blood circulation":287,"glvI, glr4197":287,"histone demethylase activity (H3-dimethyl-K4 specific)":287,"ligand-gated ion channel activity":287,"nuclear nucleosome":287,"viral capsid":287,"RIBOSOMAL PROTEIN S10":286,"RIBOSOMAL PROTEIN S11":286,"RIBOSOMAL PROTEIN S12":286,"RIBOSOMAL PROTEIN S13":286,"RIBOSOMAL PROTEIN S14":286,"RIBOSOMAL PROTEIN S16":286,"RIBOSOMAL PROTEIN S18":286,"RIBOSOMAL PROTEIN S19":286,"RIBOSOMAL PROTEIN S2":286,"RIBOSOMAL PROTEIN S20":286,"RIBOSOMAL PROTEIN S3":286,"RIBOSOMAL PROTEIN S4":286,"RIBOSOMAL PROTEIN S9":286,"RIBOSOMAL PROTEIN THX":286,"S-adenosyl-L-methionine binding":286,"SUGAR (BETA-FRUCTOSE-1,6-DIPHOSPHATE)":286,"Vaccinia virus WR":286,"activation of JUN kinase activity":286,"bidirectional double-stranded viral DNA replication":286,"decoding, Streptomycin, RNA structure, antibiotic resistance, RIBOSOME-ANTIBIOTIC complex":286,"ligand-dependent nuclear receptor binding":286,"structural constituent of ribosome":286,"(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.":285,"-!- A bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities. -!- It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates. -!- It also converts leukotriene A(4) into leukotriene B(4), unlike EC 3.2.2.10 which converts leukotriene A(4) into 5,6-dihydroxy- 7,9,11,14-eicosatetraenoic acid.":285,"Aeropyrum":285,"Aspergillus fumigatus Af293":285,"Bifunctional dihydrofolate reductase-thymidylate synthase":285,"Desulfovibrio gigas":285,"Influenza A virus (A/California/04/2009(H1N1))":285,"Leukotriene A(4) hydrolase. Leukotriene-A4 hydrolase. LTA-4 hydrolase.":285,"Leukotriene-A(4) hydrolase.":285,"NEDD8 ligase activity":285,"NMDA selective glutamate receptor complex":285,"activation of NF-kappaB-inducing kinase activity":285,"phosphatidylinositol-3,4-bisphosphate binding":285,"positive regulation of endothelial cell chemotaxis to fibroblast growth factor":285,"receptor-receptor interaction":285,"(+)-camphor + reduced putidaredoxin + O(2) = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H(2)O.":284,"-!- Also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy- 1,2-campholide.":284,"3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL":284,"Camphor 5-exo-methylene hydroxylase. Cytochrome p450-cam.":284,"Camphor 5-monooxygenase.":284,"Fibrinogen alpha chain":284,"Hepacivirus":284,"IMMUNE SYSTEM/VIRAL PROTEIN":284,"Serine hydroxymethyltransferase":284,"Small nuclear ribonucleoprotein Sm D1":284,"Small nuclear ribonucleoprotein Sm D2":284,"Transcription elongation factor B polypeptide 1":284,"Transcription elongation factor B polypeptide 2":284,"Xanthine dehydrogenase":284,"positive regulation of T cell migration":284,"positive regulation of axonogenesis":284,"xenobiotic catabolic process":284,"-!- The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3. -!- Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO(2), ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, but more slowly.":283,"Hydrolase/DNA":283,"Macaca mulatta":283,"Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O.":283,"Methane hydroxylase.":283,"Methane monooxygenase (soluble).":283,"Ribonuclease":283,"cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A":283,"establishment of mitotic spindle orientation":283,"nucleoside diphosphate kinase activity":283,"nucleotide-activated protein kinase complex":283,"oogenesis":283,"phosphatidylinositol phospholipase C activity":283,"thymus development":283,"virus tail, baseplate":283,"-!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. -!- UTP, CTP and ITP can act as donors. -!- Not identical with EC 2.7.1.105.":282,"6-phosphofructokinase.":282,"ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.":282,"ATP generation from poly-ADP-D-ribose":282,"ATP synthase subunit gamma":282,"Beta-glucosidase":282,"FAB":282,"HBB":282,"LT2 / SGSC1412 / ATCC 700720":282,"MR-1":282,"Notch binding":282,"Phosphofructokinase I. Phosphohexokinase.":282,"SF9":282,"Small nuclear ribonucleoprotein E":282,"Small nuclear ribonucleoprotein G":282,"TYROSINE":282,"branched-chain amino acid biosynthetic process":282,"pantothenate biosynthetic process":282,"positive regulation of bone mineralization":282,"toll-like receptor 4 signaling pathway":282,"-!- The enzyme from Burkholderia fungorum strain LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske- type iron-sulfur cluster and a catalytic mononuclear nonheme iron center. -!- Chlorine-substituted biphenyls can also act as substrates. -!- Similar to the three-component enzyme systems EC 1.14.12.3 and EC 1.14.12.11.":281,"1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL":281,"Aspergillus oryzae":281,"B cell proliferation":281,"Biphenyl + NADH + O(2) = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+).":281,"Biphenyl 2,3-dioxygenase.":281,"Biphenyl dioxygenase.":281,"FUMARIC ACID":281,"RIBOSOMAL PROTEIN":281,"Structural genomics, unknown function":281,"Trichoderma reesei":281,"autolysosome":281,"chloride transport":281,"endolysosome membrane":281,"excitatory synapse":281,"transcriptional activator activity, RNA polymerase II transcription factor binding":281,"-!- The plant enzyme also catalyzes the reactions of EC 2.1.3.6, EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase, converting agmatine and ornithine into putrescine and citrulline respectively.":280,"ALDH2, ALDM":280,"ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).":280,"Alcohol dehydrogenase E chain":280,"Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.":280,"Citrulline phosphorylase. Ornithine transcarbamylase. OTC. OTCase.":280,"E3 ubiquitin-protein ligase Mdm2":280,"ELECTRON TRANSPORT, IRON STORAGE, iron binding, iron mobilization, OXIDOREDUCTASE":280,"L-tyrosine-tRNA(Tyr) ligase (AMP-forming). Tyrosine translase. Tyrosine tRNA synthetase. Tyrosine-transfer ribonucleate synthetase. Tyrosine-transfer RNA ligase. Tyrosyl-transfer ribonucleate synthetase. Tyrosyl-transfer ribonucleic acid synthetase. Tyrosyl-transfer RNA synthetase. Tyrosyl-tRNA ligase. Tyrosyl-tRNA synthetase.":280,"Ornithine carbamoyltransferase.":280,"Photosystem II manganese-stabilizing polypeptide":280,"Protein RecA":280,"RNA-binding protein Hfq":280,"Tyrosine--tRNA ligase.":280,"coenzyme A biosynthetic process":280,"depyrimidination":280,"isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway":280,"mitochondrial DNA repair":280,"neutrophil mediated immunity":280,"positive regulation of plasminogen activation":280,"pyrimidine nucleoside biosynthetic process":280,"response to metal ion":280,"-!- Acts on blood group substance H. -!- Can use a number of 2-fucosyl-galactosides as acceptors.":279,"-!- Acts on blood group substance, and can use a number of 2-fucosyl- galactosides as acceptors.":279,"4-hydroxy-tetrahydrodipicolinate synthase":279,"43, gp43":279,"A transferase. Fucosylgalactose alpha-N-acetylgalactosaminyltransferase. Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase. Histo-blood group A acetylgalactosaminyltransferase. Histo-blood group A transferase.":279,"Cytochrome c oxidase polypeptide VIII-heart":279,"Cytochrome c oxidase polypeptide VIIa-heart":279,"Cytochrome c oxidase polypeptide VIIb":279,"Cytochrome c oxidase polypeptide VIIc":279,"Cytochrome c oxidase polypeptide VIa-heart":279,"Cytochrome c oxidase polypeptide Va":279,"Cytochrome c oxidase polypeptide Vb":279,"Cytochrome c oxidase subunit 6A2":279,"Cytochrome c oxidase subunit 7B":279,"Cytochrome c oxidase subunit 8B":279,"Cytochrome c-550":279,"DNA":279,"Fucosylgalactoside 3-alpha-galactosyltransferase.":279,"Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase.":279,"H2-D1":279,"Histo-blood group ABO system transferase":279,"MC2 155":279,"PYROCOCCUS FURIOSUS":279,"S-adenosylhomocysteine metabolic process":279,"Staphylococcus epidermidis":279,"UDP-N-acetyl-alpha-beta-D-galactosamine + glycoprotein-alpha-L-fucosyl- (1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl- (1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose.":279,"UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R.":279,"[Blood group substance] alpha-galactosyltransferase. B transferase. Blood-group substance alpha-dependent galactosyltransferase. Blood-group substance B-dependent galactosyltransferase. Fucosylglycoprotein 3-alpha-galactosyltransferase. Glycoprotein-fucosylgalactoside alpha-galactosyltransferase. Histo-blood group B transferase. Histo-blood substance alpha-dependent galactosyltransferase. UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose 3-alpha-D- galactosyltransferase. UDPgalactose:O-alpha-L-fucosyl(1->2)D-galactose alpha-D- galactosyltransferase.":279,"circadian regulation of gene expression":279,"histone-arginine N-methyltransferase activity":279,"induction of bacterial agglutination":279,"response to acidic pH":279,"-!- Acts on short-chain aliphatic nitriles, converting them into the corresponding acid amides. -!- Does not act on these amides or on aromatic nitriles (cf. EC 3.5.5.1).":278,"-!- The reaction is catalyzed in the opposite direction. -!- Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD(+) biosynthesis enzyme shared by both eukaryotes and prokaryotes.":278,"ATP + dTMP = ADP + dTDP.":278,"An aliphatic amide = a nitrile + H(2)O.":278,"Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3- dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate.":278,"Nicotinate-nucleotide diphosphorylase (carboxylating).":278,"Nicotinate-nucleotide pyrophosphorylase (carboxylating). Quinolinate phosphoribosyltransferase (decarboxylating).":278,"Nitrilase. Nitrile hydro-lyase.":278,"Nitrile hydratase.":278,"SRP-dependent cotranslational protein targeting to membrane":278,"Thymidylate kinase. Thymidylic acid kinase. TMPK.":278,"dTMP kinase.":278,"-!- Contains FAD. -!- All thymidylate synthases catalyze a reductive methylation involving the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5-position of dUMP and a two electron reduction of the methylene group to a methyl group. -!- Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses folate as both a 1-carbon donor and a source of reducing equivalents, this enzyme uses a flavin coenzyme as a source of reducing equivalents, which are derived from NADPH.":277,"-!- Formed from the precursor factor VII. -!- The cattle enzyme is more readily inhibited by diisopropyl fluorophosphate than the human. -!- Belongs to peptidase family S1.":277,"-!- Formerly EC 2.7.7.26 and EC 3.1.4.8.":277,"-!- S-adenosylhomocysteine can also act as donor.":277,"5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+).":277,"7,8-diamino-pelargonic acid aminotransferase. 7,8-diaminononanoate aminotransferase. Adenosylmethionine--8-amino-7-oxononanoate aminotransferase. DAPA aminotransferase.":277,"ATP synthase subunit gamma, mitochondrial":277,"Adenosylmethionine--8-amino-7-oxononanoate transaminase.":277,"Aspergillus oryzae ribonuclease. Guanyloribonuclease. Ribonuclease T1. RNase N1. RNase N2.":277,"Borrelia burgdorferi":277,"CLOSTRIDIUM PERFRINGENS":277,"Coagulation factor VIIa.":277,"Desulfovibrio vulgaris":277,"FDTS. Flavin dependent thymidylate synthase.":277,"Lactococcus phage TP901-1":277,"NADH binding":277,"Ribonuclease T(1).":277,"S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4- methylthio-2-oxobutanoate + 7,8-diaminononanoate.":277,"Thymidylate synthase (FAD).":277,"Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in G-P with 2',3'-cyclic phosphate intermediates.":277,"Zea":277,"actinin binding":277,"microfilament motor activity":277,"negative regulation of axonogenesis":277,"positive regulation of vascular smooth muscle cell proliferation":277,"pre-miRNA processing":277,"response to interleukin-6":277,"transcription regulator":277,"transferase activity, transferring acyl groups other than amino-acyl groups":277,"-!- Inorganic triphosphate can also act as donor.":276,"-!- Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. -!- Uracil-DNA glycosylase (EC 3.2.2.27) and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolyzing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalyzing the removal of mis-incorporated uracil from DNA.":276,"15692":276,"ATP + AMP = 2 ADP.":276,"Adenylate kinase.":276,"Adenylic kinase. Adenylokinase. Myokinase.":276,"Bradyrhizobium diazoefficiens USDA 110":276,"Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.":276,"THALLIUM (I) ION":276,"Uracil DNA glycohydrolase. Uracil-DNA N-glycosylase.":276,"Uracil-DNA glycosylase.":276,"alpha-amylase activity":276,"cellular response to BMP stimulus":276,"conserved hypothetical protein":276,"fructose 1,6-bisphosphate 1-phosphatase activity":276,"glyceraldehyde oxidoreductase activity":276,"intercellular bridge":276,"morphogenesis of an epithelium":276,"peptide hormone binding":276,"poly(U) RNA binding":276,"proteasome core complex":276,"small protein activating enzyme binding":276,"transcription factor catabolic process":276,"ATP synthase subunit epsilon":275,"CGA009":275,"D-alanyl-D-alanine carboxypeptidase":275,"DNA (5'-D(*CP*AP*TP*TP*AP*GP*AP*A)-3')":275,"Dihydrolipoyl dehydrogenase":275,"Geobacter sulfurreducens PCA":275,"Lactococcus lactis subsp. lactis Il1403":275,"PROLINE":275,"TRYPANOSOMA BRUCEI BRUCEI":275,"Translation factors":275,"cellular response to granulocyte macrophage colony-stimulating factor stimulus":275,"positive regulation of histone acetylation":275,"pyrF, MTH_129":275,"regulation of glucose transport":275,"regulation of insulin receptor signaling pathway":275,"18S ribosomal RNA":274,"Cytochrome c":274,"Glycogen synthase kinase-3 beta":274,"Pteridine reductase":274,"Transferase/transferase inhibitor":274,"UDP-glucuronate biosynthetic process":274,"arginase activity":274,"mannonate dehydratase activity":274,"neurotrophin TRKA receptor binding":274,"nucleosome binding":274,"protein monoubiquitination":274,"BACILLUS STEAROTHERMOPHILUS":273,"BRD4, HUNK1":273,"Dickeya dadantii 3937":273,"Transferases.":273,"UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH.":273,"UDP-glucose 6-dehydrogenase.":273,"ankyrin binding":273,"catenin complex":273,"deoxyribonucleotide biosynthetic process":273,"negative regulation of dopaminergic neuron differentiation":273,"protein targeting":273,"response to starvation":273,"ribonucleoside-diphosphate reductase complex":273,"ribosomal RNA 16S":273,"ELONGATION FACTOR G":272,"Histone H2A type 1":272,"Methanosarcina mazei":272,"PSEUDOMONAS PUTIDA":272,"Sterne":272,"bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding":272,"cytochrome-b5 reductase activity, acting on NAD(P)H":272,"fungal-type vacuole":272,"positive regulation of NK T cell activation":272,"regulation of axon extension":272,"regulation of gluconeogenesis":272,"vasculogenesis":272,"ATCC 43589 / MSB8 / DSM 3109 / JCM 10099":271,"Acting on GTP; involved in cellular and subcellular movement.":271,"Bacillus stearothermophilus":271,"Blood fluke":271,"HLA-DRB1":271,"Phanerochaete chrysosporium":271,"SUGAR (D-GALACTOSE)":271,"clawed frog,common platanna,platanna":271,"cuprous ion binding":271,"histone demethylation":271,"induction by virus of host autophagy":271,"mitotic sister chromatid segregation":271,"negative regulation of NFAT protein import into nucleus":271,"negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator":271,"negative regulation of translational initiation":271,"nitrogen fixation":271,"osteoclast differentiation":271,"positive regulation of mitochondrion organization":271,"positive regulation of protein homodimerization activity":271,"(1) UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine. (2) UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine.":270,"-!- The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.":270,"-!- Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. -!- EC 2.4.1.255 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.":270,"Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA.":270,"CD4":270,"CD4 receptor binding":270,"Glutamate decarboxylase.":270,"L-glutamate 1-carboxy-lyase.":270,"L-glutamate = 4-aminobutanoate + CO(2).":270,"O-linked N-acetylglucosaminyltransferase. OGTase.":270,"Protein O-GlcNAc transferase.":270,"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit":270,"protein O-GlcNAc transferase activity":270,"180-MERIC":269,"ER to Golgi transport vesicle":269,"Meleagris gallopavo":269,"PERK-mediated unfolded protein response":269,"PLAU":269,"Phenylalanine--tRNA ligase beta subunit":269,"Pyrobaculum":269,"dGTP catabolic process":269,"histone demethylase activity (H3-K4 specific)":269,"membrane protein":269,"negative regulation of DNA binding":269,"-!- Belongs to peptidase family S1. -!- Formerly EC 3.4.4.5 and EC 3.4.4.6.":268,"-!- The enzyme, which is found in anaerobic and facultative organisms such as bacteria, parasitic helminthes, and lower marine organisms, utilizes low potential quinols, such as menaquinol and rhodoquinol, to reduce fumarate as the final step of an anaerobic respiratory chain. -!- The enzyme is known as complex II of the electron transfer chain, similarly to EC 1.3.5.1, to which it is closely related.":268,"5' to 3' exonuclease, C-terminal subdomain":268,"Ac-Asp-Glu binding":268,"Alpha-chymotrypsin. Chymotrypsin A. Chymotrypsin B.":268,"C-terminal protein deglutamylation":268,"Chymotrypsin.":268,"Delta H":268,"Focal adhesion kinase 1":268,"Fumarate reductase (menaquinone). Succinate dehydrogenase (menaquinone).":268,"Fumarate reductase (quinol).":268,"Glutamate carboxypeptidase 2":268,"ITGB3, GP3A":268,"Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.":268,"Voltage-gated potassium channel":268,"apicoplast":268,"carboxyl- or carbamoyltransferase activity":268,"cellular response to copper ion":268,"chronological cell aging":268,"enzyme linked receptor protein signaling pathway":268,"maternal process involved in female pregnancy":268,"negative regulation of cytokine production":268,"phagocytosis, engulfment":268,"phosphopyruvate hydratase activity":268,"pore complex":268,"positive regulation of chemokine secretion":268,"positive regulation of protein dephosphorylation":268,"regulation of alternative mRNA splicing, via spliceosome":268,"sodium ion binding":268,"tetrahydrofolyl-poly(glutamate) polymer binding":268,"transferrin receptor binding":268,"-!- Formerly EC 4.1.2.15.":267,"2-dehydro-3-deoxy-phosphoheptonate aldolase. 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase. 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating). D-erythrose-4-phosphate-lyase. D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating). DAH7-P synthase. DAHP synthase. Deoxy-D-arabino-heptulosonate-7-phosphate synthetase. DHAP synthase. DS-Co. DS-Mn. KDPH synthase. KDPH synthetase. Phospho-2-dehydro-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptanoate aldolase. Phospho-2-keto-3-deoxyheptonate aldolase. Phospho-2-keto-3-deoxyheptonic aldolase. Phospho-2-oxo-3-deoxyheptonate aldolase.":267,"3-deoxy-7-phosphoheptulonate synthase.":267,"AMINOTRANSFERASE":267,"Canavalia ensiformis":267,"Heat-labile enterotoxin B chain":267,"Peroxiredoxin":267,"Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D- arabino-hept-2-ulosonate 7-phosphate + phosphate.":267,"SUS SCROFA":267,"acetyl-CoA carboxylase complex":267,"positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway":267,"-!- Acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. -!- Some EC 3.2.1.23 and EC 3.2.1.38 enzymes also hydrolyze alpha-L- arabinosides. -!- cf. EC 3.2.1.185. -!- Formerly EC 3.2.1.79.":266,"-!- Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer. -!- In addition to the above reaction, the enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent. -!- Responsible for initiating both straight- and branched-chain fatty- acid biosynthesis, with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism. -!- For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight- and branched-chain (C4--C6) acyl-CoA primers whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA.":266,"3-ketoacyl-acyl carrier protein synthase III. 3-oxoacyl:ACP synthase III. Beta-ketoacyl (acyl carrier protein) synthase III. Beta-ketoacyl-ACP synthase III. Beta-ketoacyl-acyl carrier protein synthase III. KAS III. KASIII.":266,"Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier- protein] + CoA + CO(2).":266,"Alpha-L-arabinofuranosidase. Arabinofuranosidase. Arabinosidase.":266,"Beta-ketoacyl-[acyl-carrier-protein] synthase III.":266,"G-protein coupled receptor activity":266,"Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.":266,"Methionyl-tRNA synthetase":266,"Mycobacterium abscessus ATCC 19977":266,"Non-reducing end alpha-L-arabinofuranosidase.":266,"Physeter":266,"Pseudomonas phage phi6":266,"REACTION CENTER PROTEIN H CHAIN":266,"Zymomonas mobilis":266,"cyclic-di-GMP binding":266,"endothelial cell morphogenesis":266,"frizzled binding":266,"oxaloacetate metabolic process":266,"polysaccharide digestion":266,"sperm whale":266,"tube development":266,"'de novo' protein folding":265,"Methanopyrus kandleri AV19":265,"RNA polymerase II transcription corepressor activity":265,"STREPTOMYCES CLAVULIGERUS":265,"acrosomal vesicle":265,"mushroom body development":265,"negative regulation of cellular senescence":265,"regulation of filopodium assembly":265,"suppression by virus of host RIG-I activity by RIG-I proteolysis":265,"suppression by virus of host translation initiation factor activity":265,"translational termination":265,"2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity":264,"ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).":264,"DNA topoisomerase type II (ATP-hydrolyzing) activity":264,"HORMONE RECEPTOR":264,"Ralstonia eutropha JMP134":264,"SNRPD1":264,"SNRPE":264,"Threonine translase. Threonyl-tRNA synthetase.":264,"Threonine--tRNA ligase.":264,"basal part of cell":264,"calmodulin-dependent protein kinase activity":264,"mitochondrial respiratory chain complex III":264,"poly(A) binding":264,"positive regulation of monocyte differentiation":264,"positive regulation of protein targeting to membrane":264,"production of siRNA involved in RNA interference":264,"Chymotrypsinogen A":263,"HYDROLASE/HYDROLASE Inhibitor":263,"Norwalk virus":263,"Rho GTPase binding":263,"SOLUBLE ACETYLCHOLINE RECEPTOR":263,"Thermoactinomyces vulgaris":263,"Transcription/DNA":263,"UDP-glucose 6-dehydrogenase activity":263,"axon terminus":263,"fatty acid oxidation":263,"histone deacetylation":263,"humoral immune response mediated by circulating immunoglobulin":263,"lipid A biosynthetic process":263,"negative regulation of ATPase activity":263,"negative regulation of cell migration involved in sprouting angiogenesis":263,"uncharacterized protein":263,"Burkholderia pseudomallei K96243":262,"CALCIUM-BINDING PROTEIN":262,"STAUROSPORINE":262,"T-tubule":262,"TUNGSTATE(VI)ION":262,"Tryptophan synthase alpha chain":262,"insulin-like growth factor I binding":262,"positive regulation of osteoclast differentiation":262,"positive regulation of viral release from host cell":262,"purine ribonucleoside monophosphate biosynthetic process":262,"response to epidermal growth factor":262,"transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding":262,"unidentified":262,"Escherichia coli UTI89":261,"Geobacter sulfurreducens":261,"Glutaminase.":261,"L-glutamine + H(2)O = L-glutamate + NH(3).":261,"L-glutamine amidohydrolase.":261,"L-phenylalanine catabolic process":261,"Leukotriene A-4 hydrolase":261,"Medicago truncatula":261,"Methanococcus maripaludis":261,"PIM1":261,"integral component of external side of plasma membrane":261,"leukotriene-A4 hydrolase activity":261,"mitotic metaphase plate congression":261,"negative regulation of cyclin-dependent protein serine/threonine kinase activity":261,"negative regulation of megakaryocyte differentiation":261,"-!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.":260,"-!- Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate. -!- In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm. -!- The enzyme from some species can also use NAD(+) but much more slowly.":260,"Dual-cofactor-specific isocitrate dehydrogenase. IDH. IDP. Isocitrate (NADP) dehydrogenase. Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Isocitrate dehydrogenase (NADP). Isocitrate dehydrogenase (NADP-dependent). NADP isocitric dehydrogenase. NADP(+)-ICDH. NADP(+)-IDH. NADP(+)-linked isocitrate dehydrogenase. NADP-dependent isocitrate dehydrogenase. NADP-dependent isocitric dehydrogenase. NADP-linked isocitrate dehydrogenase. NADP-specific isocitrate dehydrogenase. Oxalosuccinate decarboxylase. Oxalsuccinic decarboxylase. Triphosphopyridine nucleotide-linked isocitrate dehydrogenase- oxalosuccinate carboxylase.":260,"G-rich strand telomeric DNA binding":260,"Hepatocyte growth factor receptor":260,"Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.":260,"Isocitrate dehydrogenase (NADP(+)).":260,"MT2170, prcB, Rv2110c":260,"MtPDC (mitochondrial pyruvate dehydrogenase complex). Pyruvate decarboxylase. Pyruvate dehydrogenase. Pyruvate dehydrogenase (lipoamide). Pyruvate dehydrogenase complex. Pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- acetylating). Pyruvic acid dehydrogenase. Pyruvic dehydrogenase.":260,"Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).":260,"Pyruvate dehydrogenase (acetyl-transferring).":260,"Trypsin":260,"chromatin silencing at silent mating-type cassette":260,"establishment of skin barrier":260,"negative regulation of catalytic activity":260,"negative regulation of inclusion body assembly":260,"positive regulation of T cell differentiation":260,"positive regulation of kinase activity":260,"(2R,3R,4R,5R)-2-((1S,2S,3R,4S,6R)-4,6-DIAMINO-3-((2R,3R,6S)-3-AMINO-6-(AMINOMETHYL)-TETRAHYDRO-2H-PYRAN-2-YLOXY)-2-HYDROXYCYCLOHEXYLOXY)-5-METHYL-4-(METHYLAMINO)-TETRAHYDRO-2H-PYRAN-3,5-DIOL":259,"(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.":259,"-!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211).":259,"3-hydroxyacyl-CoA dehydrogenase.":259,"Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase.":259,"Chorismate = prephenate.":259,"Chorismate mutase.":259,"DNA gyrase subunit B":259,"DNA helicase activity":259,"Dictyostelium":259,"Helicobacter pylori J99":259,"Hydroxyphenylpyruvate synthase.":259,"Lactococcus":259,"Parabacteroides distasonis ATCC 8503":259,"REACTION CENTER PROTEIN L CHAIN":259,"REACTION CENTER PROTEIN M CHAIN":259,"SH3 domain":259,"host cell surface binding":259,"negative regulation of viral process":259,"transforming growth factor beta receptor binding":259,"-!- Wide specificity; also hydrolyzes vitamin A esters. -!- The enzymes from microsomes also catalyze the reactions of EC 3.1.1.2, EC 3.1.1.5, EC 3.1.1.6, EC 3.1.1.23, EC 3.1.1.28, EC 3.1.2.2, EC 3.5.1.4, and EC 3.5.1.13. -!- Formerly EC 3.1.1.12.":258,"A carboxylic ester + H(2)O = an alcohol + a carboxylate.":258,"Ali-esterase. B-esterase. Cocaine esterase. Methylbutyrase. Monobutyrase. Procaine esterase.":258,"Caenorhabditis":258,"Carboxylesterase.":258,"Glutamate dehydrogenase":258,"PHEOPHYTIN A":258,"S288c":258,"cell death":258,"homeostasis of number of cells":258,"negative regulation of BMP signaling pathway":258,"protection from natural killer cell mediated cytotoxicity":258,"tumor necrosis factor receptor binding":258,"-!- Guanine and 6-mercaptopurine can replace hypoxanthine.":257,"2',3'-DIDEOXYCYTIDINE 5'-TRIPHOSPHATE":257,"ANTIBIOTIC":257,"African malaria mosquito":257,"Guanine phosphoribosyltransferase. HGPRTase. Hypoxanthine-guanine phosphoribosyltransferase. IMP diphosphorylase. IMP pyrophosphorylase. Transphosphoribosidase.":257,"Hypoxanthine phosphoribosyltransferase.":257,"IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.":257,"activation of cysteine-type endopeptidase activity":257,"calcitriol binding":257,"calcitriol receptor activity":257,"gag":257,"lateral plasma membrane":257,"mismatched DNA binding":257,"negative regulation of ATP biosynthetic process":257,"-!- Belongs to peptidase family S1E.":256,"-!- The enzyme from Saccharomyces cerevisiae is highly specific for tetradecanoyl-CoA, and for N-terminal glycine in oligopeptides containing serine in the 5-position. -!- The enzyme from mammalian heart transfers acyl groups to a specific acceptor protein of 51 kDa.":256,"-!- This enzyme catalyzes the final step in methanogenesis, the biological production of methane. -!- This important anaerobic process is carried out only by methanogenic archaea. -!- The enzyme can also function in reverse, for anaerobic oxidation of methane. -!- The enzyme requires the hydroporphinoid nickel complex coenzyme F(430). -!- Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. -!- The sulfide sulfur can be replaced by selenium but not by oxygen.":256,"ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL":256,"Agrobacterium tumefaciens str.":256,"Amyloid beta A4 protein":256,"BRAF, BRAF1, RAFB1":256,"Biotin carboxylase":256,"Bombyx mori":256,"Coenzyme-B sulfoethylthiotransferase.":256,"Glycylpeptide N-tetradecanoyltransferase.":256,"Influenzavirus A":256,"Kluyveromyces lactis":256,"Methyl coenzyme M reductase. Methyl-CoM reductase.":256,"Methyl-CoM + CoB = CoM-S-S-CoB + methane.":256,"N-terminal peptidyl-lysine acetylation":256,"OXYGEN STORAGE":256,"Peptide N-myristoyltransferase. Peptide N-tetradecanoyltransferase.":256,"SNRPD2":256,"Solanum lycopersicum":256,"Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.":256,"Transferred entry: 1.17.1.4.":256,"glutamate receptor binding":256,"kinesin complex":256,"microtubule motor activity":256,"motor activity":256,"neurotransmitter receptor biosynthetic process":256,"peptidyl-serine ADP-ribosylation":256,"positive regulation of Ras protein signal transduction":256,"protein ADP-ribosylase activity":256,"regulation of cysteine-type endopeptidase activity involved in apoptotic process":256,"response to pain":256,"retinoid binding":256,"virion binding":256,"-!- Also acts on 3-hydroxykynurenine. -!- The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.":255,"-!- This enzyme, along with EC 2.5.1.59 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. -!- These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction.":255,"2-(2-METHOXYETHOXY)ETHANOL":255,"43589":255,"Ames Ancestor":255,"Blastochloris viridis":255,"CAAX farnesyltransferase. FTase.":255,"Catalytic domain":255,"Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.":255,"Kynurenine aminotransferase. Kynurenine--oxoglutarate aminotransferase.":255,"Kynurenine--oxoglutarate transaminase.":255,"L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.":255,"Photosystem II 12 kDa extrinsic protein":255,"Protein farnesyltransferase.":255,"Pyrogallol hydroxytransferase large subunit":255,"Pyrogallol hydroxytransferase small subunit":255,"Pyruvate kinase isozymes M1/M2":255,"Rhodospirillum rubrum":255,"Transferase/RNA":255,"cellular protein catabolic process":255,"establishment or maintenance of cell polarity":255,"glycogen catabolic process":255,"iron assimilation by chelation and transport":255,"microtubule bundle formation":255,"negative regulation of glycogen (starch) synthase activity":255,"negative regulation of type B pancreatic cell development":255,"phosphate-containing compound metabolic process":255,"superior temporal gyrus development":255,"tRNA modification":255,"(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier- protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].":254,"-!- Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. -!- While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme. -!- The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. -!- Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures.":254,"3-PHOSPHOGLYCERIC ACID":254,"3-oxoacyl-acyl carrier protein synthase I. Beta-ketoacyl-ACP synthase II. KAS II. KASII.":254,"Beta-ketoacyl-[acyl-carrier-protein] synthase II.":254,"CFN 42":254,"Enolase":254,"LYSOZYME C":254,"Poly [ADP-ribose] polymerase 1":254,"Ralstonia eutropha H16":254,"URIDINE 5'-TRIPHOSPHATE":254,"anaphase-promoting complex binding":254,"condensed nuclear chromosome outer kinetochore":254,"ferric iron binding":254,"hepatocyte growth factor-activated receptor activity":254,"mitochondrial DNA metabolic process":254,"negative regulation of blood coagulation":254,"negative regulation of guanyl-nucleotide exchange factor activity":254,"negative regulation of signal transduction by p53 class mediator":254,"pentose-phosphate shunt":254,"positive regulation of chondrocyte differentiation":254,"positive regulation of neutrophil chemotaxis":254,"protein targeting to membrane":254,"(GAGUU)10GAG 53-NUCLEOTIDE RNA":253,"1-THIOETHANESULFONIC ACID":253,"Chaperone protein DnaK":253,"DIHYDROFOLATE REDUCTASE":253,"DNA demethylation":253,"Protein-serine/threonine kinases.":253,"RNA processing":253,"Transferred entry: 2.7.1.191, 2.7.1.192, 2.7.1.193, 2.7.1.194, 2.7.1.195, 2.7.1.196, 2.7.1.197, 2.7.1.198, 2.7.1.199, 2.7.1.200, 2.7.1.201, 2.7.1.202, 2.7.1.203, 2.7.1.204, 2.7.1.205, 2.7.1.206, 2.7.1.207 and 2.7.1.208.":253,"UDP-galactopyranose mutase":253,"androgen metabolic process":253,"beta-tubulin binding":253,"lumenal side of lysosomal membrane":253,"mammalian, Sec61, translocation, translation, RIBOSOME":253,"negative regulation of supramolecular fiber organization":253,"positive regulation of extrinsic apoptotic signaling pathway":253,"positive regulation of myoblast differentiation":253,"protein targeting to lysosome involved in chaperone-mediated autophagy":253,"regulation of DNA recombination":253,"regulation of protein import":253,"transcription factor TFIID complex":253,"-!- Trypanothione disulfide is the oxidized form of N(1),N(8)- bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. -!- The activity is dependent on a redox-active cystine at the active center (cf. EC 1.8.1.7). -!- Formerly EC 1.6.4.8.":252,"ATP3, ATP3a, ATP3b, YBR039W, YBR0408":252,"Acinetobacter sp. ADP1":252,"Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O(2).":252,"HYDROLASE/ANTIBIOTIC":252,"L-asparaginase":252,"L-cysteine catabolic process":252,"M17 leucyl aminopeptidase":252,"N(1),N(8)-bis(glutathionyl)spermidine reductase. NADPH:trypanothione oxidoreductase. Trypanothione reductase.":252,"Pseudomonas syringae pv. tomato":252,"Purine nucleoside phosphorylase DeoD-type":252,"PyrD":252,"Ran GTPase binding":252,"TRIOSEPHOSPHATE ISOMERASE":252,"Trypanothione + NADP(+) = trypanothione disulfide + NADPH.":252,"Trypanothione reductase":252,"Trypanothione-disulfide reductase.":252,"UNP RESIDUES 2-62":252,"UNP RESIDUES 23-160":252,"UNP RESIDUES 34-311":252,"UNP RESIDUES 34-511":252,"UNP RESIDUES 36-545":252,"glycosome":252,"ion channel activity":252,"molybdopterin molybdotransferase activity":252,"negative regulation of actin filament polymerization":252,"negative regulation of endothelial cell migration":252,"post-embryonic development":252,"-!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1.":251,"-!- This enzyme, along with EC 2.5.1.58 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. -!- These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. -!- The Zn(2+) is required for peptide, but not for isoprenoid, substrate binding.":251,"10 kDa chaperonin":251,"3-enol-pyruvoylshikimate-5-phosphate synthase. 5-enolpyruvylshikimate-3-phosphate synthase. EPSP synthase.":251,"3-phosphoshikimate 1-carboxyvinyltransferase.":251,"ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC ACID":251,"ASA dehydrogenase. Aspartic semialdehyde dehydrogenase. L-aspartate-beta-semialdehyde dehydrogenase.":251,"Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.":251,"Aspartate-semialdehyde dehydrogenase.":251,"FE-MO-S CLUSTER":251,"GGTase-I. GGTaseI. Type I protein geranyl-geranyltransferase.":251,"Glucose phosphomutase. Phosphoglucose mutase.":251,"HYBRIDOMA":251,"KT2440":251,"L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH.":251,"MOLYBDENUM ATOM":251,"PCC 7421":251,"Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate.":251,"Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).":251,"Protein geranylgeranyltransferase type I.":251,"SERINE PROTEASE":251,"Thymidylate kinase":251,"euchromatin":251,"glucose binding":251,"kinesin binding":251,"peptidyl-lysine modification":251,"Burkholderia cenocepacia":250,"CYTOCHROME B":250,"Candida":250,"EGFR, ERBB, ERBB1, HER1":250,"Fab Heavy Chain":250,"HA, hemagglutinin":250,"Influenza A virus (A/Puerto Rico/8/1934(H1N1))":250,"N-terminal protein amino acid modification":250,"Peroxisomal primary amine oxidase":250,"RISC complex":250,"Tyrosine-protein kinase JAK2":250,"hematopoietic progenitor cell differentiation":250,"positive regulation of chemokine biosynthetic process":250,"response to methylmercury":250,"tRNA methylation":250,"1-deoxy-D-xylulose 5-phosphate reductoisomerase":249,"DNA topoisomerase type I activity":249,"Escherichia virus Lambda":249,"GTP + H(2)O = GDP + phosphate.":249,"H(+)/Cl(-) exchange transporter ClcA":249,"Mu50 / ATCC 700699":249,"Neisseria gonorrhoeae FA 1090":249,"Thermococcus":249,"actin-dependent ATPase activity":249,"high-density lipoprotein particle":249,"negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway":249,"positive regulation of endothelial cell apoptotic process":249,"protein kinase, inhibitor, TRANSFERASE-TRANSFERASE INHIBITOR complex":249,"sterol metabolic process":249,"transcription factor import into nucleus":249,"CARBONIC ANHYDRASE II":248,"Cytochrome b559 subunit alpha":248,"Cytochrome c oxidase polypeptide 7A1":248,"Cytochrome c oxidase subunit VIb isoform 1":248,"DNA (28-MER)":248,"GLYCOPROTEIN":248,"Gelsolin":248,"Klebsiella aerogenes":248,"Nostoc sp.":248,"Putative oxidoreductase":248,"Queuine tRNA-ribosyltransferase":248,"STREPTAVIDIN":248,"Transcription regulator":248,"diadenosine tetraphosphate biosynthetic process":248,"dog":248,"lysophospholipase activity":248,"nuclear envelope disassembly":248,"oligosaccharide binding":248,"positive regulation of apoptotic signaling pathway":248,"regulation of axonogenesis":248,"ubiquitin conjugating enzyme activity":248,"-!- The enzyme catalyzes a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone. -!- The animal, but not the plant, form of the enzyme is inhibited by dicoumarol. -!- Formerly EC 1.6.99.2.":247,"11-CYCLOPROPYL-5,11-DIHYDRO-4-METHYL-6H-DIPYRIDO[3,2-B:2',3'-E][1,4]DIAZEPIN-6-ONE":247,"Aldehyde-lyases.":247,"Azoreductase. Dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone). Diaphorase. DT-diaphorase. Flavoprotein NAD(P)H-quinone reductase. Menadione oxidoreductase. Menadione reductase. NAD(P)H dehydrogenase. NAD(P)H menadione reductase. NAD(P)H(2) dehydrogenase (quinone). NAD(P)H-quinone dehydrogenase. NAD(P)H-quinone oxidoreductase. NAD(P)H: menadione oxidoreductase. NAD(P)H:(quinone-acceptor)oxidoreductase. NADH-menadione reductase. Naphthoquinone reductase. p-benzoquinone reductase. Phylloquinone reductase. Quinone reductase. Reduced NAD(P)H dehydrogenase. Reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase. Viologen accepting pyridine nucleotide oxidoreductase. Vitamin K reductase. Vitamin-K reductase.":247,"Bcl-2 family protein complex":247,"Bordetella bronchiseptica":247,"Glucose-1-phosphate thymidylyltransferase.":247,"HMGCR":247,"NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone.":247,"NAD(P)H dehydrogenase (quinone).":247,"RNA (77-MER)":247,"Serotransferrin":247,"Tyrosine-protein kinase SYK":247,"UV-damage excision repair":247,"barbed-end actin filament capping":247,"dTDP-glucose diphosphorylase. dTDP-glucose pyrophosphorylase. dTDP-glucose synthase.":247,"dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose.":247,"fatty acid catabolic process":247,"hemagglutinin":247,"natural killer cell activation":247,"porin activity":247,"regulation of NMDA receptor activity":247,"-!- Acts on [acyl-carrier-protein] thioesters of fatty acids from C(12) to C(18), but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested.":246,"-!- The enzyme acts on the hydroxy group of the hydrated derivative of the substrate. -!- Formerly EC 1.2.1.14.":246,"-!- Was previously thought to be a copper protein, but it is now known that the enzymes from soybean (Glycine max), the mold Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. -!- The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO(2), although there is an enzyme-catalyzed pathway in which EC 3.5.2.17 catalyzes the first step. -!- The enzyme is different from EC 1.14.13.113.":246,"-!- Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH. -!- The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.":246,"Acyl-[acyl-carrier-protein] hydrolase. S-acyl fatty acid synthase thioesterase.":246,"Avermectin-sensitive glutamate-gated chloride channel GluCl alpha":246,"CAAX-protein geranylgeranyltransferase complex":246,"Factor independent urate hydroxylase.":246,"Glycoaldehyde transferase.":246,"IMP dehydrogenase.":246,"IMP oxidoreductase. Inosinate dehydrogenase. Inosine 5'-monophosphate dehydrogenase. Inosine monophosphate oxidoreductase. Inosinic acid dehydrogenase.":246,"Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH.":246,"Mouse monoclonal Fab fragment, heavy chain":246,"Mouse monoclonal Fab fragment, light chain":246,"Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate.":246,"Oleoyl-[acyl-carrier-protein] hydrolase.":246,"Photosystem II reaction center protein K":246,"Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.":246,"Synechococcus elongatus PCC 6301":246,"Transketolase.":246,"Urate + O(2) + H(2)O = 5-hydroxyisourate + H(2)O(2).":246,"Urate oxidase. Uric acid oxidase. Uricase. Uricase II.":246,"early endosome to late endosome transport":246,"evasion or tolerance by virus of host immune response":246,"fungal-type cell wall organization":246,"intracellular pH elevation":246,"regulation of microtubule polymerization":246,"regulation of protein localization to nucleus":246,"-!- Also hydrolyzes alpha-D-fucosides.":245,"ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL":245,"Alpha-galactosidase.":245,"Carboxy-lyases.":245,"HYDROLASE/PROTEIN BINDING":245,"Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha- D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.":245,"Melibiase.":245,"Photosystem II reaction center protein H":245,"Photosystem II reaction center protein Z":245,"SUMO binding":245,"Vibrio cholerae O395":245,"Viral protein/Immune system":245,"actin filament severing":245,"cadherin binding involved in cell-cell adhesion":245,"cytosolic large ribosomal subunit":245,"detoxification of copper ion":245,"positive regulation of innate immune response":245,"regulation of nucleotide-binding oligomerization domain containing signaling pathway":245,"regulation of protein import into nucleus, translocation":245,"Great pond snail":244,"HIV-1 REVERSE TRANSCRIPTASE":244,"NMDA glutamate receptor activity":244,"Nitrite reductase":244,"POLYETHYLENE GLYCOL (N=34)":244,"UDP-N-acetylglucosamine biosynthetic process":244,"adhesion of symbiont to host":244,"cGMP catabolic process":244,"chitin binding":244,"mitogen-activated protein kinase kinase binding":244,"opsonization":244,"positive regulation of protein import into nucleus":244,"(1) Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. (2) Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine(34) in tRNA + guanine.":243,"-!- Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. -!- In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. -!- In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ(1), which is ultimately modified to queuine. -!- The eubacterial enzyme can also use an earlier intermediate, preQ(0), to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn). -!- This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway.":243,"1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE":243,"Arginase-1":243,"Elongation factor 2":243,"Guanine insertion enzyme. Q-insertase. Queuine tRNA-ribosyltransferase. Queuine(34) transfer ribonucleate ribosyltransferase. TGT. tRNA guanine(34) transglycosidase. tRNA transglycosylase.":243,"HLA-DRA, HLA-DRA1":243,"Heme oxidase. Heme oxygenase. Heme oxygenase (decyclizing).":243,"NK T cell differentiation":243,"Ogataea angusta":243,"Thioredoxin 1":243,"Vibrio vulnificus":243,"cellular response to exogenous dsRNA":243,"cellular response to follicle-stimulating hormone stimulus":243,"cellular response to misfolded protein":243,"negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway":243,"protein complex disassembly":243,"response to inorganic substance":243,"response to lipid":243,"spliceosomal tri-snRNP complex assembly":243,"tRNA-guanine(34) transglycosylase.":243,"BETA-TRYPSIN":242,"Bacteroides vulgatus ATCC 8482":242,"California sea hare":242,"DNA ligase":242,"Mandelate racemase/muconate lactonizing protein":242,"Probable peroxiredoxin":242,"RHA1":242,"RNA polymerase omega chain":242,"Rana catesbeiana":242,"SOD1":242,"Streptococcus agalactiae":242,"acetylcholine receptor binding":242,"exogenous drug catabolic process":242,"histone H4 deacetylation":242,"ligand binding domain":242,"protein farnesyltransferase activity":242,"response to cytokinin":242,"sperm capacitation":242,"tetrahydrofolate interconversion":242,"uracil DNA N-glycosylase activity":242,"-!- A class of enzymes that remove acetyl groups from N(6)-acetyl-lysine residues on a histone. -!- The reaction of this enzyme is opposite to that of EC 2.3.1.48. -!- Histone deacetylases (HDACs) can be organized into three classes depending on sequence similarity and domain organization. -!- Histone acetylation plays an important role in regulation of gene expression. -!- In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation. -!- May be identical to EC 3.5.1.17.":241,"-!- Subtilisin is a serine endopeptidase that evolved independently of chymotrypsin. -!- It contains no cysteine residues (although these are found in homologous enzymes). -!- Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase C, nagarse, nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). -!- Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species. -!- Belongs to peptidase family S8. -!- Formerly EC 3.4.4.16 and EC 3.4.21.14.":241,"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.":241,"2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl- D-erythritol 2,4-cyclodiphosphate + CMP.":241,"Aspergillus niger":241,"Concanavalin-A":241,"Desulfovibrio":241,"Endoglucanase":241,"HDAC.":241,"Histone deacetylase.":241,"Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.":241,"Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.":241,"MECDP-synthase.":241,"MHC class I antigen":241,"Pd 1222":241,"RNA strand annealing activity":241,"Subtilisin.":241,"Uricase":241,"androgen binding":241,"cell division site":241,"cellular response to peptide hormone stimulus":241,"chordate embryonic development":241,"histone H3-Y41 phosphorylation":241,"histone kinase activity (H3-Y41 specific)":241,"interleukin-12-mediated signaling pathway":241,"mitochondrial membrane":241,"positive regulation of DNA biosynthetic process":241,"response to interleukin-12":241,"retinoic acid binding":241,"skeletal muscle tissue development":241,"transforming growth factor beta-activated receptor activity":241,"-!- Essential, along with EC 2.3.1.39, for the initiation of fatty-acid biosynthesis in bacteria. -!- The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide. -!- This is one of the activities associated with EC 2.3.1.180.":240,"ACAT. Acetyl coenzyme A-acyl-carrier-protein transacylase. ACP acetyltransferase. Acyl-carrier-protein acetyltransferase.":240,"Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier- protein].":240,"HELICOBACTER PYLORI":240,"Hirudo medicinalis":240,"RESIDUES 1-1732":240,"[Acyl-carrier-protein] S-acetyltransferase.":240,"activation of protein kinase C activity":240,"antigen processing and presentation of peptide antigen":240,"negative regulation of cell differentiation":240,"negative regulation of tumor necrosis factor (ligand) superfamily member 11 production":240,"nucleosomal histone binding":240,"positive regulation of bone mineralization involved in bone maturation":240,"regulation of mitotic metaphase/anaphase transition":240,"-!- May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. -!- Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.":239,"-!- This eukaryotic enzyme catalyzes the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. -!- Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. -!- The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues. -!- PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells. -!- Cf. EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322. -!- Formerly EC 2.1.1.23, EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126.":239,"2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.":239,"3937":239,"40S RIBOSOMAL PROTEIN S8":239,"Circadian clock protein kinase KaiC":239,"Cul4B-RING E3 ubiquitin ligase complex":239,"DNA-formamidopyrimidine glycosylase.":239,"Fapy-DNA glycosylase. Formamidopyrimidine-DNA glycosylase.":239,"Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.":239,"Nostoc":239,"RNA polymerase sigma factor SigA":239,"Tb10.70.6470":239,"Type I protein arginine methyltransferase.":239,"positive regulation of Notch signaling pathway":239,"positive regulation of macrophage chemotaxis":239,"regulation of attachment of spindle microtubules to kinetochore":239,"2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL":238,"40S RIBOSOMAL PROTEIN S3A":238,"Bradyrhizobium japonicum":238,"C-terminal protein amino acid modification":238,"DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT":238,"HTH-type transcriptional regulator QacR":238,"HXB2":238,"Human herpesvirus 1":238,"MALATE LIKE INTERMEDIATE":238,"Porphyromonas gingivalis":238,"RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1":238,"Rhopdopsin 7-helix transmembrane proteins":238,"SPERMIDINE":238,"Trimeric":238,"maintenance of translational fidelity":238,"nuclear envelope lumen":238,"retinoic acid receptor signaling pathway":238,"trans-Golgi network transport vesicle":238,"BIPHENYL DIOXYGENASE SUBUNIT ALPHA":237,"BIPHENYL DIOXYGENASE SUBUNIT BETA":237,"CDK2, CDKN2":237,"Cellvibrio japonicus Ueda107":237,"Dihydrodipicolinate synthase":237,"Flavin-dependent thymidylate synthase":237,"Methylamine utilization protein MauG":237,"TNKS2, PARP5B, TANK2, TNKL":237,"TRYPANOSOMA BRUCEI":237,"chondrocyte differentiation":237,"establishment of cell polarity":237,"fructose-bisphosphate aldolase activity":237,"modulation by virus of host morphology or physiology":237,"negative regulation of cell motility":237,"negative regulation of kinase activity":237,"negative regulation of reactive oxygen species metabolic process":237,"phosphoenolpyruvate carboxykinase (GTP) activity":237,"positive regulation of interleukin-17 production":237,"pseudopodium":237,"972 / ATCC 24843":236,"Acetyl-CoA carboxylase":236,"Chemotaxis protein CheY":236,"Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)":236,"TRANSFERASE/INHIBITOR":236,"TRANSPORT":236,"Tryptophan synthase beta chain":236,"apical junction assembly":236,"cellular response to indole-3-methanol":236,"mitochondrial depolarization":236,"negative regulation of phospholipase C activity":236,"positive regulation of actin filament binding":236,"positive regulation of interleukin-8 biosynthetic process":236,"positive regulation of microtubule binding":236,"response to growth factor":236,"(5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate.":235,"3-oxoacyl-[acyl-carrier-protein] synthase 1":235,"3-oxoacyl-[acyl-carrier-protein] synthase 3":235,"3-phosphoinositide-dependent protein kinase 1":235,"3-phosphoinositide-dependent protein kinase activity":235,"PGD2 synthase. PGH-PGD isomerase. Prostaglandin D synthetase. Prostaglandin D2 synthase. Prostaglandin endoperoxide Delta-isomerase. Prostaglandin-H(2) Delta-isomerase.":235,"Prostaglandin-D synthase.":235,"THYMIDINE-5'-PHOSPHATE":235,"embryonic cranial skeleton morphogenesis":235,"fusA":235,"glutamate-ammonia ligase activity":235,"maintenance of protein location in cell":235,"positive regulation of cellular metabolic process":235,"prostaglandin-D synthase activity":235,"regulation of cardiac muscle contraction":235,"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase":234,"3-hydroxyacyl-CoA dehydrogenase activity":234,"30S ribosomal subunit, Ribosome, Kasugamycin, KsgA, RNA structure, Thermus thermophilus, Antibiotic resistance, Decoding":234,"ATP + NAD(+) = ADP + NADP(+).":234,"CYCLIN-A2":234,"Candida glabrata CBS 138":234,"DPN kinase.":234,"Fusarium oxysporum":234,"Glucose-1-phosphate thymidylyltransferase":234,"MLL3/4 complex":234,"NAD(+) kinase.":234,"Steroid Delta-isomerase":234,"cellular response to nerve growth factor stimulus":234,"dynein intermediate chain binding":234,"o-succinylbenzoate synthase":234,"receptor-mediated endocytosis of virus by host cell":234,"regulation of cell-cell adhesion":234,"transcription":234,"-!- In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. -!- In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon- amino group of an L-lysine residue of the acceptor protein.":233,"-!- This enzyme phosphorylates and activates its downstream protein kinase, EC 2.7.12.2, but requires MAPKKKK for activation. -!- Some members of this family can be activated by p21-activated kinases (PAK/STE20) or Ras. -!- While c-Raf and c-Mos activate the classical MAPK/ERK pathway, MEKK1 and MEKK2 preferentially activate the c-Jun N-terminal protein kinase(JNK)/stress-activated protein kinase (SAPK) pathway. -!- Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. -!- Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury. -!- Formerly EC 2.7.1.37.":233,"Canis":233,"EGG":233,"Fibroblast growth factor receptor 1":233,"HECT E3 ligase. Ubiquitin transferase HECT-E3.":233,"HECT-type E3 ubiquitin transferase.":233,"JUN kinase binding":233,"Legionella pneumophila":233,"Lipase":233,"Lysine-specific demethylase 4A":233,"MAP kinase kinase kinase. MAP3K. MAPKKK. MEK kinase. MEKK. MLK-like mitogen-activated protein triple kinase. MLTK.":233,"Mitogen-activated protein kinase kinase kinase.":233,"Mycobacterium tuberculosis H37Ra":233,"Novosphingobium aromaticivorans":233,"PCC 7120":233,"Pseudomonas aeruginosa UCBPP-PA14":233,"Retinoic acid receptor RXR-alpha":233,"Streptomyces aureofaciens":233,"hydrolase/DNA":233,"negative regulation of Ras protein signal transduction":233,"negative regulation of mitochondrial depolarization":233,"positive regulation of CREB transcription factor activity":233,"protein N-linked glycosylation":233,"regulation of multicellular organism growth":233,"transferase/DNA":233,"ventral cord development":233,"3-CYCLOHEXYL-1-PROPYLSULFONIC ACID":232,"Aminopeptidase":232,"Canis lupus":232,"DNA N-glycosylase activity":232,"DNA catabolic process":232,"MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN":232,"MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII":232,"MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN":232,"MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN":232,"MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C":232,"MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2":232,"MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I":232,"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)":232,"OLEIC ACID":232,"PLACENTA":232,"Ruminiclostridium thermocellum":232,"THYMIDYLATE SYNTHASE":232,"UNP RESIDUES 77-272":232,"cellular response to cytokine stimulus":232,"eosinophil chemotaxis":232,"glutamate secretion":232,"negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway":232,"nitric oxide synthase, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex":232,"positive regulation of viral process":232,"regulation of phosphorelay signal transduction system":232,"response to selenium ion":232,"retinal dehydrogenase activity":232,"thioredoxin-disulfide reductase activity":232,"vitamin D binding":232,"Acting on acid anhydrides.":231,"Cul5-RING ubiquitin ligase complex":231,"FUNGAL, DEHYDRATASE, ENOYL REDUCTASE, KETOACYL SYNTHASE, KETOACYL REDUCTASE, MALONYL/PALMITOYL TRANSFERASE, TRANSFERASE, SUBSTRATE SHUTTLING, MULTIFUNCTIONAL ENZYME, ACYL CARRIER PROTEIN, FATTY ACID SYNTHESIS, ACETYL TRANSFERASE, FATTY ACID SYNTHASE":231,"ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)":231,"MAP kinase-activated protein kinase 2":231,"b0344, JW0335, lacZ":231,"clathrin-coated vesicle":231,"cobalamin metabolic process":231,"embryonic digestive tract development":231,"negative regulation of DNA recombination":231,"negative regulation of glycolytic process":231,"negative regulation of proteasomal ubiquitin-dependent protein catabolic process":231,"positive regulation of exosomal secretion":231,"spleen development":231,"Adenylosuccinate synthase.":230,"Adenylosuccinate synthetase. IMP--aspartate ligase. Succinoadenylic kinosynthetase.":230,"BICINE":230,"Brevibacterium flavum":230,"GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)- AMP.":230,"Histone H2B":230,"I-SMAD binding":230,"N-acetylneuraminate lyase":230,"NADPH regeneration":230,"RHODOBACTER CAPSULATUS":230,"S-adenosylmethionine synthase":230,"Streptococcus suis":230,"Trp ligands":230,"actomyosin":230,"endothelial cell proliferation":230,"intermediate filament cytoskeleton":230,"positive regulation by symbiont of host protein levels":230,"positive regulation of lamellipodium morphogenesis":230,"positive regulation of transcription initiation from RNA polymerase II promoter":230,"synaptic cleft":230,"vasculature development":230,"(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H(2)O.":229,"-!- Appears to be distinct from other protein phosphokinases. -!- Brings about multiple phosphorylation of the unique C-terminal repeat domain of the largest subunit of eukaryotic EC 2.7.7.6. -!- Does not phosphorylate casein, phosvitin or histone. -!- Formerly EC 2.7.1.141.":229,"-!- Forms part of the vitamin-K biosynthesis pathway.":229,"2-succinylbenzoate synthase. o-succinylbenzoic acid synthase. OSB synthase. OSBS.":229,"ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.":229,"BP-1":229,"Beta-xylanase":229,"CTD kinase.":229,"HSRV2":229,"Jelly Rolls":229,"Paracoccus":229,"Scapharca inaequivalvis":229,"With other acceptors.":229,"[RNA-polymerase]-subunit kinase.":229,"branching involved in ureteric bud morphogenesis":229,"familiaris":229,"muscle alpha-actinin binding":229,"o-succinylbenzoate synthase.":229,"positive regulation of nuclear-transcribed mRNA poly(A) tail shortening":229,"racemase and epimerase activity":229,"response to aluminum ion":229,"response to progesterone":229,"soybean":229,"-!- Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.":228,"-!- The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage.":228,"-!- These enzymes form some of the cyclic phosphate Ins(cyclic 1,2)P(4,5)P(2) as well as Ins(1,4,5)P(3). -!- They show activity toward phosphatidylinositol, i.e., the activity of EC 4.6.1.13 in vitro at high calcium concentration.":228,"1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion.":228,"1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.":228,"1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase. Monophosphatidylinositol phosphodiesterase. Phosphatidylinositol phospholipase C. Phosphoinositidase C. PI-PLC. Triphosphoinositide phosphodiesterase.":228,"300-MERIC":228,"Acanthamoeba polyphaga mimivirus":228,"Aequorea":228,"Alkyl-DHAP synthase. Alkyldihydroxyacetonephosphate synthase.":228,"Alkylglycerone-phosphate synthase.":228,"Catalyzes the rearrangement of -S-S- bonds in proteins.":228,"Chaetomium thermophilum":228,"Ino80 complex":228,"M band":228,"Methionyl-tRNA synthetase, putative":228,"Phosphoinositide phospholipase C.":228,"Protein disulfide-isomerase.":228,"S-S rearrangase.":228,"TSP-1 type 1 repeat":228,"Thaumatococcus daniellii":228,"acyl-CoA metabolic process":228,"alkylglycerone-phosphate synthase activity":228,"disulfide oxidoreductase activity":228,"endogenous lipid antigen binding":228,"ether lipid biosynthetic process":228,"glycosaminoglycan catabolic process":228,"low-density lipoprotein particle binding":228,"platelet-derived growth factor receptor signaling pathway":228,"positive regulation of JAK-STAT cascade":228,"positive regulation of endocytosis":228,"protein modification process":228,"regulation of vascular permeability":228,"response to manganese ion":228,"-!- Cf. EC 3.2.1.41 and EC 3.2.1.57.":227,"-!- Glycerone and L-glyceraldehyde can act as acceptors. -!- UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors.":227,"-!- Wide specificity for D-amino acids. -!- Also acts on glycine.":227,"2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE":227,"A D-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).":227,"ACETOACETYL-COENZYME A":227,"ATP + glycerol = ADP + sn-glycerol 3-phosphate.":227,"ATP:glycerol 3-phosphotransferase. Glycerokinase.":227,"Chromobacterium violaceum":227,"D-amino-acid oxidase":227,"D-amino-acid oxidase.":227,"DSM 3638":227,"Fibronectin":227,"Gamma-aminobutyric-acid receptor subunit beta-1":227,"Glycerol kinase":227,"Glycerol kinase.":227,"Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).":227,"LEISHMANIA MAJOR":227,"MONOTHIOGLYCEROL":227,"N-TERMINAL DOMAIN":227,"NADPH--cytochrome P450 reductase":227,"Neopullulanase.":227,"T7-like viruses":227,"early phagosome":227,"fatty-acyl-CoA biosynthetic process":227,"negative regulation of DNA replication":227,"positive regulation of RNA splicing":227,"positive regulation of protein complex disassembly":227,"BETA-2 MICROGLOBULIN":226,"Bartonella henselae str. Houston-1":226,"GLUTAMINE SYNTHETASE":226,"GOLD ION":226,"LEAD (II) ION":226,"Lambda-like viruses":226,"SUGAR (ALPHA D-GALACTOSE)":226,"TCR-alpha":226,"TCR-beta":226,"enzyme inhibitor activity":226,"host cell plasma membrane":226,"phosphatidic acid biosynthetic process":226,"positive regulation of membrane protein ectodomain proteolysis":226,"positive regulation of translational elongation":226,"protein deacetylase activity":226,"regulation of cytokine production":226,"regulation of protein localization to cell surface":226,"sodium ion transmembrane transport":226,"vascular endothelial growth factor binding":226,"-!- This enzyme is important for the maintenance of the correct reading frame during translation. -!- Unlike TrmD from Escherichia coli, which recognizes the G(36)pG(37) motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37. -!- Formerly EC 2.1.1.31.":225,"Aldolase class I":225,"Glr4197 protein":225,"Glycylpeptide N-tetradecanoyltransferase":225,"HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4":225,"S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA.":225,"Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A":225,"Transfer RNA (m(1)G(37)) methyltransferase. tRNA (m(1)G(37)) methyltransferase. tRNA-(N(1)G37) methyltransferase.":225,"branched-chain-amino-acid transaminase activity":225,"hormone activity":225,"induction of positive chemotaxis":225,"negative regulation of B cell proliferation":225,"positive regulation of insulin secretion":225,"striated muscle contraction":225,"tRNA (guanine(37)-N(1))-methyltransferase.":225,"(R,R)-2,3-BUTANEDIOL":224,"B cell homeostasis":224,"CD38":224,"DNA polymerase iota":224,"Formamidopyrimidine-DNA glycosylase":224,"MALATE DEHYDROGENASE":224,"Major prion protein":224,"NONAN-1-OL":224,"PHENOL":224,"Serine/threonine-protein kinase PLK1":224,"Shigella":224,"Zika virus":224,"axonal fasciculation":224,"leopard danio,zebra danio,zebra fish":224,"mitotic chromosome condensation":224,"peptide N-acetyltransferase activity":224,"positive regulation of killing of cells of other organism":224,"ubiquinone binding":224,"-!- D-glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act as acceptors. -!- ITP and dATP can act as donors.":223,"ATP + D-hexose = ADP + D-hexose 6-phosphate.":223,"Adenylate kinase":223,"Bacillus licheniformis DSM 13 = ATCC 14580":223,"DNA replication initiation":223,"DNA unwinding involved in DNA replication":223,"DODECAETHYLENE GLYCOL":223,"Hexokinase type I. Hexokinase type II. Hexokinase type III. Hexokinase type IV (glucokinase).":223,"Hexokinase.":223,"Low-density Lipoprotein Receptor":223,"PDE10A":223,"SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT":223,"UREA":223,"cellular response to fibroblast growth factor stimulus":223,"chloride channel activity":223,"multivesicular body assembly":223,"myosin V binding":223,"negative regulation of protein secretion":223,"neuroepithelial cell differentiation":223,"other organism cell membrane":223,"peptidyl-lysine monomethylation":223,"phagocytosis, recognition":223,"positive regulation of vascular permeability":223,"regulation of dendrite morphogenesis":223,"response to host immune response":223,"response to nitrosative stress":223,"retinoic acid receptor activity":223,"-!- Involved in histidine biosynthesis.":222,"-!- This mammalian enzyme participates in the degradation of heme. -!- The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. -!- The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. -!- The enzyme requires NAD(P)H and EC 1.6.2.4. -!- Cf. EC 1.14.15.20. -!- Formerly EC 1.14.99.3.":222,"Actin-related protein 2/3 complex subunit 2":222,"Citrate synthase":222,"Enterobacter cloacae subsp. cloacae ATCC 13047":222,"FOLIC ACID":222,"Heme oxygenase (biliverdin-producing).":222,"LAURIC ACID":222,"Methanopyrus kandleri":222,"OXAMIC ACID":222,"Peroxidase":222,"Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform":222,"Proliferating cell nuclear antigen":222,"Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O.":222,"RESIDUES 47-528":222,"SUGAR (N-ACETYL-D-GALACTOSAMINE)":222,"Thymidine kinase":222,"cardiac muscle hypertrophy":222,"mitotic sister chromatid cohesion":222,"negative regulation of transforming growth factor-beta secretion":222,"nitric oxide dioxygenase activity":222,"nitrite reductase (cytochrome, ammonia-forming) activity":222,"positive regulation of interferon-gamma secretion":222,"release of sequestered calcium ion into cytosol":222,"sequestering of actin monomers":222,"-!- The gamma-carboxymide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N(6)-(5-glutamyl)lysine crosslinks.":221,"1,4-dihydroxy-2-naphthoyl-CoA synthase activity":221,"ADENOSINE-3'-5'-DIPHOSPHATE":221,"Fibrinoligase. Glutaminylpeptide gamma-glutamyltransferase. Polyamine transglutaminase. TGase. Transglutaminase.":221,"Laccase":221,"OXIDOREDUCTASE/INHIBITOR":221,"Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH(3).":221,"Protein-glutamine gamma-glutamyltransferase.":221,"RIBOSOME, HIRSH TRNA":221,"TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID":221,"Thaumatin-1":221,"androgen receptor signaling pathway":221,"carbon catabolite repression of transcription":221,"coenzyme A metabolic process":221,"maltose-transporting ATPase activity":221,"mesenchymal cell differentiation":221,"oxygen homeostasis":221,"positive regulation of SMAD protein import into nucleus":221,"queuosine biosynthetic process":221,"regulation of mitotic spindle organization":221,"response to sucrose":221,"ribosomal large subunit export from nucleus":221,"spliceosomal snRNP assembly":221,"supramolecular fiber organization":221,"-!- Also catalyzes acyloin formation.":220,"2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE":220,"2-oxo-acid carboxy-lyase. Alpha-carboxylase. Alpha-ketoacid carboxylase. Pyruvic decarboxylase.":220,"60S ribosomal protein L30":220,"A 2-oxo acid = an aldehyde + CO(2).":220,"Chitinase":220,"DNA (5'-D(*TP*CP*TP*AP*AP*TP*G)-3')":220,"Fiber protein":220,"I-kappaB phosphorylation":220,"Integrin alpha-IIb":220,"PPARG, NR1C3":220,"Pyruvate decarboxylase.":220,"Streptomyces griseus":220,"Succinate dehydrogenase cytochrome b560 subunit, mitochondrial":220,"TRANSCRIPTION, TRANSCRIPTION INITIATION":220,"Thermosynechococcus vulcanus":220,"UA159":220,"actin filament reorganization":220,"detection of virus":220,"promoter-specific chromatin binding":220,"(S)-malate = fumarate + H(2)O.":219,"700699":219,"ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).":219,"Actin-related protein 2/3 complex subunit 3":219,"DNA protection":219,"Fumarase.":219,"Fumarate hydratase.":219,"Glutamate receptor ionotropic, kainate 2":219,"Glyoxylase III.":219,"LIGAND BINDING PROTEIN":219,"Micromonospora echinospora":219,"Periplasmic [NiFe] hydrogenase small subunit":219,"Pol polyprotein":219,"Proline translase. Prolyl-tRNA synthetase.":219,"Proline--tRNA ligase.":219,"acetyl-CoA binding":219,"apical cortex":219,"microspike assembly":219,"positive regulation of interleukin-4 biosynthetic process":219,"regulation of T cell activation":219,"ribosomal small subunit export from nucleus":219,"tetrahydrofolate metabolic process":219,"-!- The enzyme oxidizes aliphatic monoamines and diamines, histamine and ethanolamine, but not secondary and tertiary amines, quaternary ammonium salts or aromatic amines. -!- Formerly EC 1.4.98.1 and EC 1.4.99.3.":218,"-!- This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. -!- (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. -!- In many bacterial species, both activities are carried out by a single bifunctional enzyme. -!- The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. -!- NADP(+) can also act as acceptor, but with lower activity. -!- Formerly EC 1.5.1.12.":218,"1-pyrroline-5-carboxylate dehydrogenase. Delta(1)-pyrroline-5-carboxylate dehydrogenase. Pyrroline-5-carboxylate dehydrogenase.":218,"AMO":218,"ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His).":218,"Actin-related protein 2/3 complex subunit 4":218,"Actin-related protein 2/3 complex subunit 5":218,"Amine dehydrogenase. MADH. Methylamine dehydrogenase. Primary-amine dehydrogenase.":218,"Cul4A-RING E3 ubiquitin ligase complex":218,"Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.":218,"Heparin-binding growth factor 1":218,"Histidine translase. Histidyl-tRNA synthetase.":218,"Histidine--tRNA ligase.":218,"Immunoglobulin G-binding protein A":218,"L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH.":218,"L-glutamate gamma-semialdehyde dehydrogenase.":218,"Methylamine + H(2)O + 2 oxidized [amicyanin] = formaldehyde + NH(3) + 2 reduced [amicyanin].":218,"Methylamine dehydrogenase (amicyanin).":218,"Mycobacterium marinum M":218,"NAD+ kinase activity":218,"RNA cap binding":218,"Vascular endothelial growth factor A":218,"cellular zinc ion homeostasis":218,"negative regulation of cell-matrix adhesion":218,"positive regulation of microtubule nucleation":218,"positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress":218,"suppression by virus of host apoptotic process":218,"-!- Also acts on N-glycoloylneuraminate, and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.":217,"ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1":217,"Glycine":217,"Inosine-5'-monophosphate dehydrogenase":217,"K12 substr. MG1655":217,"KIDNEY":217,"N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate.":217,"N-acetylneuraminate lyase.":217,"N-acetylneuraminate pyruvate-lyase. N-acetylneuraminic acid aldolase.":217,"RACK1":217,"T-cell receptor beta-2 chain C region":217,"Thermoanaerobacter tengcongensis":217,"Tissue factor":217,"Ubiquinol-cytochrome C reductase complex 14 kDa protein":217,"Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C":217,"cellular response to interleukin-4":217,"choline catabolic process":217,"cya":217,"deoxyribonucleotide catabolic process":217,"miRNA loading onto RISC involved in gene silencing by miRNA":217,"negative regulation of osteoclast differentiation":217,"nuclear periphery":217,"ossification":217,"transmembrane receptor protein tyrosine phosphatase activity":217,"-!- A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.":216,"-!- The mammalian enzymes act more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols.":216,"BIFUNCTIONAL EPOXIDE HYDROLASE 2":216,"Bordetella bronchiseptica RB50":216,"C58 / ATCC 33970":216,"Catechol O-methyltransferase.":216,"DNA repair complex":216,"Dihydrolipoamide S-succinyltransferase. Dihydrolipoamide succinyltransferase. Dihydrolipoic transsuccinylase. Dihydrolipolyl transsuccinylase. Dihydrolipoyl transsuccinylase. Lipoate succinyltransferase. Lipoic transsuccinylase. Lipoyl transsuccinylase. Succinyl-CoA:dihydrolipoamide S-succinyltransferase. Succinyl-CoA:dihydrolipoate S-succinyltransferase.":216,"Dihydrolipoyllysine-residue succinyltransferase.":216,"GROWTH FACTOR":216,"L10 Ribosomal Protein":216,"L15 Ribosomal Protein":216,"L37Ae 50S ribosomal protein":216,"Pden_4730":216,"S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol.":216,"Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine.":216,"T cell selection":216,"Tyrosine-protein kinase HCK":216,"clathrin-coated endocytic vesicle":216,"intracellular organelle":216,"low-density lipoprotein particle remodeling":216,"mdlC":216,"phosphopyruvate hydratase complex":216,"positive regulation of interleukin-4 production":216,"thylakoid":216,"-!- Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.":215,"5-phosphoribose isomerase. D-ribose-5-phosphate ketol-isomerase. Phosphopentoseisomerase. Phosphopentosisomerase. Phosphoriboisomerase. Ribose 5-phosphate epimerase. Ribose phosphate isomerase.":215,"ATCC 39315 / El Tor Inaba N16961":215,"Adenosylmethionine-8-amino-7-oxononanoate aminotransferase":215,"Aminotransferase":215,"BACE1, BACE":215,"D-amino-acid oxidase activity":215,"D-ribose 5-phosphate = D-ribulose 5-phosphate.":215,"Enterococcus faecium":215,"GTP-binding nuclear protein Ran":215,"MU-OXO-DIIRON":215,"PTB domain binding":215,"REN":215,"Ribose-5-phosphate isomerase.":215,"Serine/threonine-protein kinase/endoribonuclease IRE1":215,"UV protection":215,"antigen processing and presentation, exogenous lipid antigen via MHC class Ib":215,"bicarbonate binding":215,"positive regulation of NK T cell differentiation":215,"positive regulation of macrophage differentiation":215,"positive regulation of smoothened signaling pathway":215,"progesterone metabolic process":215,"rRNA N-glycosidase":215,"regulation of immature T cell proliferation in thymus":215,"stereocilium":215,"(1) N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (2) (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide.":214,"-!- Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5- aminoimidazole.":214,"9,9'-[(2R,3R,3AS,5S,7AR,9R,10R,10AS,12S,14AR)-3,5,10,12-TETRAHYDROXY-5,12-DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,2-D:3',2'-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-2,9-DIYL]BIS(2-AMINO-1,9-DIHYDRO-6H-PURIN-6-ONE)":214,"ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126":214,"Adenylosuccinase. Succino AMP-lyase.":214,"Adenylosuccinate lyase":214,"Adenylosuccinate lyase.":214,"Bordetella pertussis":214,"CB15":214,"COENZYME B":214,"Escherichia virus P1":214,"Major capsid protein":214,"MetI-like":214,"Penicillin + H(2)O = a carboxylate + 6-aminopenicillanate.":214,"Penicillin acylase.":214,"Penicillin amidase.":214,"STREPTOCOCCUS PYOGENES":214,"Set1C/COMPASS complex":214,"TETRAFLUOROMAGNESATE(2-)":214,"Tyrosine--tRNA ligase":214,"URACIL":214,"acid phosphatase activity":214,"maintenance of DNA methylation":214,"nuclear-transcribed mRNA catabolic process":214,"outer membrane":214,"positive regulation of I-kappaB phosphorylation":214,"positive regulation of cysteine-type endopeptidase activity":214,"renal water homeostasis":214,"-!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25.":213,"23857":213,"ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL":213,"Coagulation factor XI":213,"DNA (146-MER)":213,"NLS-bearing protein import into nucleus":213,"Rossmann fold, OXIDOREDUCTASE":213,"Streptomyces cattleya":213,"actin cortical patch":213,"carAa":213,"endosome to lysosome transport":213,"methyl-CpG binding":213,"oxidoreductase activity, acting on other nitrogenous compounds as donors":213,"phosphoserine binding":213,"photosynthesis":213,"positive regulation of interleukin-1 beta secretion":213,"potassium ion transmembrane transport":213,"rough endoplasmic reticulum":213,"-!- The enzyme shows no activity with D-galactonate. -!- Cf. EC 4.2.1.140.":212,"Alkaline phosphatase":212,"Barrel medic":212,"D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H(2)O.":212,"E264 / ATCC 700388 / DSM 13276 / CIP 106301":212,"Enoyl-[acyl-carrier-protein] reductase [NADPH]":212,"FGF1, FGFA":212,"Fibroblast growth factor receptor 2":212,"Gluconate dehydratase.":212,"Janthinobacterium":212,"NAD+ nucleosidase activity":212,"Rhodnius prolixus":212,"Superoxide dismutase [Mn]":212,"Translation initiation factor 2 subunit gamma":212,"Vibrio harveyi":212,"embryo development":212,"isolate BH10":212,"maize":212,"positive regulation of cation channel activity":212,"production of miRNAs involved in gene silencing by miRNA":212,"response to X-ray":212,"ribonucleoprotein complex":212,"siRNA binding":212,"telomeric repeat-containing RNA binding":212,"transcription factor activity, RNA polymerase II transcription factor recruiting":212,"voltage-gated potassium channel activity":212,"-!- See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/ -!- Formerly EC 2.1.1.73.":211,"-!- This is a large group of enzymes, most of which form so-called 'restriction-modification systems', with nucleases that possess similar site specificity (the nucleases are listed as either EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5). -!- See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/":211,"60S ribosomal protein L3":211,"CYTOKINE/CYTOKINE RECEPTOR":211,"Cytosine 5-methyltransferase. Cytosine DNA methylase. Cytosine DNA methyltransferase. Cytosine-specific DNA methyltransferase. Deoxyribonucleate methylase. Deoxyribonucleate methyltransferase. Deoxyribonucleic (cytosine-5-)-methyltransferase. Deoxyribonucleic acid (cytosine-5-)-methyltransferase. Deoxyribonucleic acid methylase. Deoxyribonucleic acid methyltransferase. Deoxyribonucleic acid modification methylase. Deoxyribonucleic methylase. DNA 5-cytosine methylase. DNA cytosine C(5) methylase. DNA cytosine methylase. DNA methylase. DNA methyltransferase. DNA transmethylase. DNA-cytosine 5-methylase. DNA-cytosine methyltransferase. Methylphosphotriester-DNA methyltransferase. Modification methylase. Restriction-modification system. Site-specific DNA-methyltransferase (cytosine-specific). Type II DNA methylase.":211,"DIOXYGENASE":211,"DNA (cytosine-5-)-methyltransferase.":211,"EGD-e":211,"Enoyl-CoA hydratase":211,"Flavodoxin":211,"Modification methylase. N-6 adenine-specific DNA methylase. Restriction-modification system.":211,"Nicotinate-nucleotide pyrophosphorylase [carboxylating]":211,"Peptidyl-prolyl cis-trans isomerase":211,"S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.":211,"S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.":211,"Site-specific DNA-methyltransferase (adenine-specific).":211,"T-complex protein 1 subunit gamma":211,"UBIQUINONE-2":211,"cellular response to antibiotic":211,"evasion or tolerance of host immune response":211,"fructose 6-phosphate metabolic process":211,"fungal-type cell wall":211,"positive regulation of epithelial cell proliferation involved in wound healing":211,"regulation of neuron apoptotic process":211,"spectrin binding":211,"-!- A family of serine- and threonine-specific protein kinases that depend on lipids for activity. -!- They can be activated by calcium but have a requirement for the second messenger diacylglycerol. -!- Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell- signaling pathways. -!- Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumor promoters. -!- Formerly EC 2.7.1.37.":210,"-!- The enzyme from Oxalobacter formigenes can also catalyze the transfer of CoA from formyl-CoA to succinate.":210,"1-phosphatidylinositol binding":210,"9-cis retinoic acid receptor activity":210,"ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.":210,"Calcium-dependent protein kinase C. Calcium-independent protein kinase C. Calcium/phospholipid dependent protein kinase. CPKC. NPKC. PKC.":210,"Chromohalobacter salexigens":210,"Cytochrome b559 subunit beta":210,"Formyl-CoA + oxalate = formate + oxalyl-CoA.":210,"Formyl-CoA oxalate CoA-transferase. Formyl-coenzyme A transferase.":210,"Formyl-CoA transferase.":210,"HEME DOMAIN, RESIDUES 40-482":210,"HYPOXANTHINE":210,"MALATE ION":210,"Membrane protein":210,"PDZ domain":210,"Phosphoenolpyruvate carboxykinase, cytosolic [GTP]":210,"Phosphoglycerate kinase.":210,"Photosystem II reaction center protein J":210,"Protein kinase C.":210,"R-SMAD binding":210,"TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1":210,"TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2":210,"Tetronarce californica":210,"URANYL (VI) ION":210,"Vitamin D3 receptor":210,"actin filament depolymerization":210,"cAMP-activated global transcriptional regulator CRP":210,"glucokinase activity":210,"microvillus assembly":210,"peptidyl-lysine dimethylation":210,"positive regulation of cardiac muscle hypertrophy":210,"positive regulation of leukocyte migration":210,"sphingosine biosynthetic process":210,"voltage-gated potassium channel complex":210,"3-DEHYDROQUINATE DEHYDRATASE":209,"5'-DEOXYADENOSINE":209,"CSNK2A1, CK2A1":209,"Campylobacter jejuni subsp. jejuni":209,"DNA topoisomerase 1":209,"Enterobacteria phage lambda":209,"Photosystem II reaction center protein M":209,"Pseudomonas resinovorans":209,"RNA polymerase binding":209,"Transketolase":209,"cell junction assembly":209,"negative regulation of vascular permeability":209,"neurotransmitter binding":209,"positive regulation of glycolytic process":209,"regulation of BMP signaling pathway":209,"regulation of exocytosis":209,"regulation of translational initiation":209,"transaminase activity":209,"(1) Protein N(6),N(6)-dimethyl-L-lysine + 2-oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO(2). (2) Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).":208,"-!- A dual-specific protein kinase and requires mitogen-activated protein kinase kinase kinase (MAPKKK) for activation. -!- It is required for activation of EC 2.7.11.24. -!- Phosphorylation of MEK1 by Raf involves phosphorylation of two serine residues. -!- Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. -!- Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury.":208,"-!- Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys-36. -!- Lysine residues exist in three methylation states (mono-, di- and trimethylated). -!- The enzyme preferentially demethylates the dimethyl form of Lys-36 (K36me2), which is its natural substrate, to form the monomethyl and unmethylated forms of Lys-36. -!- It can also demethylate the monomethyl- but not the trimethyl form of Lys-36.":208,"-!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3).":208,"60S ribosomal protein L10":208,"Alkyldihydroxyacetonephosphate synthase, peroxisomal":208,"CA10":208,"Citrate condensing enzyme. Citrate synthetase. Citric synthase. Citric-condensing enzyme. Citrogenase. CoA-acetylating citrate oxaloacetate-lyase. Condensing enzyme. Oxalacetic transacetase. Oxaloacetate transacetase.":208,"Citrate synthase (unknown stereospecificity).":208,"FACTOR 430":208,"FTL":208,"Glutathione S-transferase A1":208,"H3-K36-specific demethylase. Histone demethylase. Histone-lysine (H3-K36) demethylase. JHDM1A. JmjC domain-containing histone demethylase 1A.":208,"ISOMERASE/DNA":208,"Immunoglobulin G-binding protein G":208,"J3":208,"MAP kinase kinase. MAP2K. MAPKK. MEK. MKK.":208,"Mitogen-activated protein kinase kinase.":208,"Ricin":208,"Spermidine synthase":208,"THALE CRESS":208,"TRANSCRIPTION/RNA/DNA":208,"UNP residues 44-359":208,"Yersinia enterocolitica":208,"[Histone H3]-lysine-36 demethylase.":208,"adenyl nucleotide binding":208,"chorismate mutase activity":208,"endothelial cell chemotaxis":208,"estrous cycle":208,"guanylate kinase activity":208,"lamellipodium assembly":208,"positive regulation of cellular response to amino acid starvation":208,"rhodopsin mediated signaling pathway":208,"-!- The proenzyme XI is activated by EC 3.4.21.38. -!- Belongs to peptidase family S1.":207,"Bacteriophage RB69":207,"Coagulation factor XIa.":207,"Cytochrome c iso-1":207,"EIF1":207,"Ferritin, middle subunit":207,"Grb2-EGFR complex":207,"Orthopoxvirus":207,"Plasma thromboplastin antecedent.":207,"Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.":207,"Shikimate dehydrogenase (NADP(+))":207,"Soluble cytochrome b562":207,"TRANSFERASE, LYASE/DNA":207,"TRYPANOTHIONE REDUCTASE":207,"Wolinella succinogenes DSM 1740":207,"Xanthomonas axonopodis pv. citri str. 306":207,"biotin metabolic process":207,"cellular response to forskolin":207,"cellular response to manganese ion":207,"glucocorticoid biosynthetic process":207,"lactate metabolic process":207,"nerve growth factor binding":207,"phosphoenolpyruvate-dependent sugar phosphotransferase system":207,"positive regulation of calcium ion transport":207,"protein folding in endoplasmic reticulum":207,"protein geranylgeranylation":207,"regulation of androgen receptor signaling pathway":207,"-!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3. -!- This is also the case for two of the four isoenzymes in Arabidopsis thaliana. -!- The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction.":206,"50S ribosomal protein L44e":206,"ATP + L-aspartate = ADP + 4-phospho-L-aspartate.":206,"Aspartate kinase.":206,"Aspartokinase.":206,"Chitinase A":206,"Chloramphenicol Acetyltransferase":206,"Chromohalobacter salexigens DSM 3043":206,"Cytochrome b-c1 complex subunit 7":206,"Human poliovirus 1":206,"NAD(P)H dehydrogenase (quinone) activity":206,"RNA":206,"Streptococcus sp. 'group G'":206,"endothelial tube morphogenesis":206,"fungal-type vacuole membrane":206,"nonhomologous end joining complex":206,"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors":206,"positive regulation of interleukin-5 production":206,"transport protein":206,"4-hydroxy-3-methylbut-2-enyl diphosphate reductase":205,"7":205,"CLOSTRIDIUM THERMOCELLUM":205,"DEAD/H-box RNA helicase binding":205,"DNA duplex unwinding":205,"DNA helicase RuvA subunit, C-terminal domain":205,"ICAM-3 receptor activity":205,"LTA4H, LTA4":205,"Methane monooxygenase component A gamma chain":205,"RNA polymerase II transcriptional preinitiation complex assembly":205,"TETRAHYMENA THERMOPHILA":205,"Transport Protein":205,"Zoogloea ramigera":205,"filopodium assembly":205,"hydrolase activity, hydrolyzing O-glycosyl compounds":205,"innate immune response-activating signal transduction":205,"integrin alphaL-beta2 complex":205,"leukocyte degranulation":205,"leukocyte migration involved in immune response":205,"negative regulation of ryanodine-sensitive calcium-release channel activity":205,"negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning":205,"potassium ion transport":205,"protein K11-linked ubiquitination":205,"regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum":205,"respiratory burst after phagocytosis":205,"response to ischemia":205,"response to steroid hormone":205,"thioredoxin peroxidase activity":205,"transcriptional repressor activity, bacterial-type RNA polymerase core promoter proximal region sequence-specific binding":205,"-!- Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 and EC 4.3.1.23 and EC 4.3.1.25. -!- The enzyme from some species is highly specific for phenylalanine. -!- Formerly EC 4.3.1.5.":204,"ATP-dependent chromatin remodeling":204,"Cupriavidus necator":204,"DIHYDROGENPHOSPHATE ION":204,"L-phenylalanine = trans-cinnamate + ammonia.":204,"Nitric oxide synthase":204,"Nitrosomonas europaea":204,"Phenylalanine ammonia-lyase.":204,"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha":204,"RESIDUES 21-119":204,"SUGAR (FRUCTOSE)":204,"T-complex protein 1 subunit beta":204,"TCEB1":204,"TCEB2":204,"Terminal oxygenase component of carbazole":204,"actin filament capping":204,"aroD, aroQ, MT2612, MTCY159.19, Rv2537c":204,"establishment of Golgi localization":204,"fat cell differentiation":204,"ferrous iron import across plasma membrane":204,"glutamate metabolic process":204,"isolate FcB1 / Columbia":204,"lateral element":204,"nitrogen catabolite repression of transcription":204,"response to yeast":204,"retinoic acid-responsive element binding":204,"-!- In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates. -!- In the absence of EC 6.3.2.6, the reaction is reversible. -!- The substrate is readily converted into 5-amino-1-(5-phospho-D- ribosyl)imidazole by non-enzymic decarboxylation.":203,"-!- Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate.":203,"30382":203,"4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.":203,"4-aminobutyrate aminotransferase. Beta-alanine--oxoglutarate aminotransferase. GABA transaminase. Gamma-amino-N-butyrate transaminase.":203,"4-aminobutyrate--2-oxoglutarate transaminase.":203,"5-(carboxyamino)imidazole ribonucleotide mutase.":203,"5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate.":203,"ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482":203,"Anabaena variabilis ATCC 29413":203,"Annexin A5":203,"Bifidobacterium longum":203,"Burkholderia cepacia":203,"ERWINIA CHRYSANTHEMI":203,"Globin-1":203,"IRON STORAGE":203,"LITHIUM ION":203,"N(5)-CAIR mutase. N(5)-carboxyaminoimidazole ribonucleotide mutase.":203,"N-acetylneuraminate catabolic process":203,"N5-carboxyaminoimidazole ribonucleotide mutase":203,"RNA-dependent RNA polymerase":203,"Ribosome/antibiotic":203,"SNARE complex":203,"Serine endoprotease DegS":203,"Sulfolobus acidocaldarius":203,"Sulfolobus shibatae B12":203,"UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose.":203,"UDP-galactopyranose mutase.":203,"UNP RESIDUES 45-76":203,"actin crosslink formation":203,"cellular bud tip":203,"protein tag":203,"protein-glutamine gamma-glutamyltransferase activity":203,"vitamin metabolic process":203,"3-deoxy-D-manno-octulosonate 8-phosphate + H(2)O = 3-deoxy-D-manno- octulosonate + phosphate.":202,"3-deoxy-manno-octulosonate-8-phosphatase.":202,"60S ribosomal protein L5":202,"Anas platyrhynchos":202,"BURKHOLDERIA XENOVORANS":202,"CARBON DIOXIDE":202,"Cd1d1, Cd1.1":202,"METHOTREXATE":202,"NCTC 9343":202,"ORF1":202,"Pancreatic alpha-amylase":202,"Penicillin G acylase":202,"Pentosyltransferases.":202,"Probable ATP-dependent RNA helicase DDX58":202,"Triosephosphate isomerase, glycosomal":202,"adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway":202,"condensed chromosome":202,"cytoplasmic microtubule":202,"embryo development ending in seed dormancy":202,"membrane fusion":202,"positive regulation of protein linear polyubiquitination":202,"profilin binding":202,"regulation of protein processing":202,"toxin catabolic process":202,"vasodilation":202,"(2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE":201,"-!- Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. -!- The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. -!- The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate.":201,"-!- The Pseudomonas enzyme is a cytochrome, but the enzyme from Micrococcus halodenitrificans is an iron protein containing molybdenum. -!- Reduced benzyl viologen and other dyes bring about the reduction of nitrate.":201,"-!- The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6, and EC 6.5.1.7.":201,"1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE":201,"Clostridium perfringens str. 13":201,"Cul3-RING ubiquitin ligase complex":201,"DNA POLYMERASE IV":201,"DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (NAD(+)). Polydeoxyribonucleotide synthase (NAD+). Polynucleotide ligase (NAD(+)). Polynucleotide ligase (NAD+).":201,"DNA ligase (NAD(+)).":201,"Deoxyuridine 5'-triphosphate nucleotidohydrolase":201,"L-phenylalanine metabolic process":201,"Large T antigen":201,"Macrophage metalloelastase":201,"Mycobacterium abscessus":201,"N-acetylglucosamine-1-phosphate uridyltransferase. UDP-N-acetylglucosamine pyrophosphorylase.":201,"NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.":201,"NUCLEUS":201,"Nitrate reductase.":201,"Nitrite + acceptor = nitrate + reduced acceptor.":201,"Pseudomonas protegens Pf-5":201,"RNA strand":201,"Respiratory nitrate reductase.":201,"SUGAR (2-PHOSPHOGLYCOLIC ACID)":201,"Streptococcus faecalis":201,"Streptomyces avermitilis MA-4680 = NBRC 14893":201,"Tryptophanyl-tRNA synthetase":201,"UDP-N-acetylglucosamine diphosphorylase.":201,"UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine.":201,"Ubiquinol-cytochrome C reductase complex 11 kDa protein":201,"Ubiquinol-cytochrome C reductase complex 7.2 kDa protein":201,"adherens junction assembly":201,"chaperone":201,"dGTP binding":201,"geranyltranstransferase activity":201,"orotidine-5'-phosphate decarboxylase activity":201,"phosphatidylinositol-3-phosphate binding":201,"ruffle organization":201,"(+)-muconolactone = cis,cis-muconate.":200,"-!- Also acts, in the reverse reaction, on 3-methyl-cis,cis-muconate and, very slowly, on cis,trans-muconate. -!- Not identical with EC 5.5.1.7 or EC 5.5.1.11.":200,"-!- The enzyme from from the bacterium Mycobacterium smegmatis is specific for maltose. -!- It has no activity with alpha-D-glucose. -!- Formerly EC 2.4.1.n5.":200,"60S ribosomal protein L28":200,"60S ribosomal protein L32":200,"60S ribosomal protein L39":200,"ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL":200,"ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu).":200,"Alpha-1,4-glucan:maltose-1-P maltosyltransferase. GMPMT.":200,"Alpha-maltose 1-phosphate + ((1->4)-alpha-D-glucosyl)(n) = phosphate + ((1->4)-alpha-D-glucosyl)(n+2).":200,"Arachis hypogaea":200,"Beta-2 microglobulin":200,"Botulinum neurotoxin type A":200,"CALMODULIN":200,"CAVIA PORCELLUS":200,"Cis,cis-muconate lactonizing enzyme I. Muconate cycloisomerase I. Muconate lactonizing enzyme.":200,"Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.":200,"Leucine translase. Leucyl-tRNA synthetase.":200,"Leucine--tRNA ligase.":200,"Macrophage elastase.":200,"Major vault protein":200,"Matrix metalloproteinase 12. Metalloelastase.":200,"Muconate cycloisomerase.":200,"POTENTIAL":200,"RPB7, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7":200,"SYK":200,"Salmonella virus P22":200,"Starch synthase (maltosyl-transferring).":200,"TRANSTHYRETIN":200,"Tryptophan--tRNA ligase":200,"chloride transmembrane transport":200,"cytoplasmic pattern recognition receptor signaling pathway in response to virus":200,"dGTPase activity":200,"dimethylallyltranstransferase activity":200,"groES protein":200,"hyaluronan catabolic process":200,"insulin-like growth factor binding":200,"iron-sulfur-molybdenum cluster with interstitial carbon":200,"myeloid cell differentiation":200,"non-membrane spanning protein tyrosine phosphatase activity":200,"positive regulation of regulatory T cell differentiation":200,"protein localization to nuclear envelope":200,"regulation of type III interferon production":200,"virus tail, fiber":200,"-!- Active at a high pH optimum. -!- Wide specificity. -!- Also catalyzes transphosphorylations. -!- Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1).":199,"-!- Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. -!- Inhibited by chelating agents. -!- Previously regarded as identical with EC 3.1.1.2.":199,"-!- Group of enzymes whose specificity is directed mainly toward the exohydrolysis of 1,4-alpha-glucosidic linkages, and that hydrolyze oligosaccharides rapidly, relative to polysaccharides, which are hydrolyzed relatively slowly, or not at all. -!- The intestinal enzyme also hydrolyzes polysaccharides, catalyzing the reactions of EC 3.2.1.3, and, more slowly, hydrolyzes 1,6-alpha-D- glucose links.":199,"-!- The enzyme from higher eukaryotes also catalyzes the reaction listed as EC 4.1.1.23.":199,"A-esterase. Aryltriphosphatase. Paraoxon hydrolase. Paraoxonase. Phosphotriesterase.":199,"Acid maltase. Glucoinvertase. Glucosidosucrase. Lysosomal alpha-glucosidase. Maltase. Maltase-glucoamylase.":199,"Actin-related protein 2/3 complex subunit 1B":199,"Alkaline phosphatase.":199,"Alkaline phosphomonoesterase. Glycerophosphatase. Phosphomonoesterase.":199,"Alpha-glucosidase.":199,"An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.":199,"Aryldialkylphosphatase.":199,"COP9 signalosome":199,"Fumarate hydratase class II":199,"GEOBACILLUS STEAROTHERMOPHILUS":199,"Glutamate receptor ionotropic, kainate 1":199,"Guanine nucleotide-binding protein G(i) subunit alpha-1":199,"Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.":199,"OPRT. Orotidine-5'-phosphate diphosphorylase. Orotidine-5'-phosphate pyrophosphorylase. Orotidylic acid phosphorylase.":199,"Orotate phosphoribosyltransferase.":199,"Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.":199,"Rhodospirillum rubrum ATCC 11170":199,"SMAD protein complex assembly":199,"cell separation after cytokinesis":199,"cellular response to parathyroid hormone stimulus":199,"cytoplasmic dynein complex":199,"methionine biosynthetic process":199,"negative regulation of G1/S transition of mitotic cell cycle":199,"positive regulation by virus of viral protein levels in host cell":199,"positive regulation of BMP signaling pathway":199,"positive regulation of histone ubiquitination":199,"sperm flagellum":199,"striated muscle thin filament":199,"(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL":198,"-!- The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. -!- The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. -!- The enzyme complex is found in aerobic bacteria, archeae, fungi and plants.":198,"60S ribosomal protein L25":198,"Brucella melitensis bv. 1 str. 16M":198,"Clostridium pasteurianum":198,"D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H(2)O + phosphate.":198,"DNA damage-binding protein 1":198,"DNA non-template strand":198,"DNA-directed RNA polymerase subunit D":198,"Galactowaldenase. UDP-galactose 4-epimerase. Uridine diphosphate galactose 4-epimerase. Uridine diphospho-galactose-4-epimerase.":198,"Glutamate--tRNA ligase":198,"HLA class I histocompatibility antigen, B-35 alpha chain":198,"MAFF303099":198,"OROTIC ACID":198,"Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing).":198,"RNA-BINDING PROTEIN":198,"SIGNALING PROTEIN, TRANSFERASE":198,"Titin":198,"UDP-alpha-D-glucose = UDP-alpha-D-galactose.":198,"UDP-glucose 4-epimerase.":198,"alpha-Man-II, GmII":198,"calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules":198,"dihydrolipoyl dehydrogenase activity":198,"glutamate decarboxylase activity":198,"interaction with host via substance in symbiont surface":198,"mauG, Pden_4736":198,"mitochondrial electron transport, cytochrome c to oxygen":198,"phospholipase A2 activity":198,"positive regulation of CD4-positive, alpha-beta T cell proliferation":198,"recognition of apoptotic cell":198,"regulation of neuron death":198,"response to UV-B":198,"suppression by virus of host mRNA export from nucleus":198,"-!- Unlike EC 1.6.5.2, this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. -!- Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17-beta-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor. -!- This enzyme can catalyze both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced. -!- Formerly EC 1.10.99.2.":197,"1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D- ribofuranosyl)nicotinamide + a quinol.":197,"11-beta-hydroxysteroid dehydrogenase.":197,"54-meric":197,"ATP SYNTHASE GAMMA CHAIN":197,"An 11-beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + NADPH.":197,"CYTIDINE-5'-DIPHOSPHATE":197,"Corticosteroid 11-beta-dehydrogenase isozyme 1":197,"Corticosteroid 11-beta-dehydrogenase.":197,"DNA mismatch repair protein MutS":197,"I band":197,"IMMUNE SYSTEM/HYDROLASE":197,"MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2":197,"N-ribosyldihydronicotinamide dehydrogenase (quinone). NQO(2). NRH:quinone oxidoreductase 2. QR2. Quinone reductase 2.":197,"Nicotiana":197,"Nitrile hydratase subunit beta":197,"Ribosyldihydronicotinamide dehydrogenase (quinone).":197,"Ribosyldihydronicotinamide dehydrogenase [quinone]":197,"ankyrin repeat binding":197,"cell cortex region":197,"dihydronicotinamide riboside quinone reductase activity":197,"histone H4 acetylation":197,"immunoglobulin complex, circulating":197,"invadopodium":197,"isocitrate dehydrogenase (NADP+) activity":197,"liver":197,"melatonin binding":197,"positive regulation of cell motility":197,"positive regulation of interleukin-6 secretion":197,"protein K6-linked ubiquitination":197,"purine nucleobase binding":197,"resveratrol binding":197,"viral nucleocapsid":197,"-!- The enzyme from most aerobic organisms is devoid of redox-active centers but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centers, flavin and a molybdenum center. -!- Together with EC 1.12.1.2, forms a system previously known as formate hydrogenlyase.":196,"Androgen receptor":196,"Brucella melitensis":196,"CYTOCHROME C PEROXIDASE":196,"Formate + NAD(+) = CO(2) + NADH.":196,"Formate dehydrogenase.":196,"GTP-dependent protein binding":196,"Hepatocyte growth factor":196,"Methanosarcina barkeri str. Fusaro":196,"Muconate cycloisomerase":196,"NADP biosynthetic process":196,"O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate.":196,"OGT":196,"Periplasmic oligopeptide-binding protein":196,"Phosphoserine phosphatase.":196,"UNP residues 23-292":196,"cellular aldehyde metabolic process":196,"heme catabolic process":196,"hepatocyte apoptotic process":196,"negative regulation of mRNA splicing, via spliceosome":196,"positive regulation of podosome assembly":196,"positive regulation of protein autophosphorylation":196,"positive regulation of small GTPase mediated signal transduction":196,"spliceosomal complex assembly":196,"starch catabolic process":196,"synaptic vesicle exocytosis":196,"tRNA (guanine-N(1)-)-methyltransferase":196,"transferase activity, transferring acyl groups":196,"-!- Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. -!- It also acts on adenosine 2'-phosphate (but not the 3'- or 5'-phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate, but does not act on inositol bisphosphates or more phosphorylated inositols.":195,"-!- Formerly EC 3.4.12.5, EC 3.4.17.7 and EC 3.4.19.10.":195,"-!- It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.":195,"-!- Uses molecular hydrogen for the reduction of a variety of substances.":195,"15993":195,"2-ketoglutarate dehydrogenase. 2-oxoglutarate dehydrogenase. 2-oxoglutarate: lipoate oxidoreductase. 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor- succinylating). AKGDH. Alpha-ketoglutarate dehydrogenase. Alpha-ketoglutaric acid dehydrogenase. Alpha-ketoglutaric dehydrogenase. Alpha-oxoglutarate dehydrogenase. Ketoglutaric dehydrogenase. OGDC. Oxoglutarate decarboxylase. Oxoglutarate dehydrogenase. Oxoglutarate dehydrogenase (lipoamide).":195,"2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).":195,"5'-DEOXY-5'-METHYLTHIOADENOSINE":195,"60-MERIC":195,"ATCC 15993":195,"ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).":195,"BPP":195,"Candida glabrata":195,"DNA glycosidase II. DNA-3-methyladenine glycosidase II.":195,"DNA-3-methyladenine glycosylase II.":195,"DNA-templated transcription, termination":195,"E264":195,"Ferredoxin--NADP reductase":195,"H(2) + A = AH(2).":195,"H(2) producing hydrogenase. Hydrogen-lyase. Hydrogenlyase. Uptake hydrogenase.":195,"Hydrogenase (acceptor).":195,"Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.":195,"Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.":195,"Inositol 1-phosphatase. Inositol monophosphate phosphatase. Inositol phosphatase. Inositol-1(or 4)-monophosphatase. L-myo-inositol-1-phosphate phosphatase. Myo-inositol 1-phosphatase. Myo-inositol monophosphatase. Myo-inositol-1(or 4)-monophosphatase. Myo-inositol-1(or 4)-phosphate phosphohydrolase. Myo-inositol-1-phosphatase.":195,"Inositol-phosphate phosphatase.":195,"Lysine translase. Lysyl-tRNA synthetase.":195,"Lysine--tRNA ligase.":195,"Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.":195,"N-acetylmuramoyl-L-alanine amidase.":195,"Neisseria meningitidis serogroup B":195,"Oxoglutarate dehydrogenase (succinyl-transferring).":195,"Structural genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, unknown function":195,"T-complex protein 1 subunit alpha":195,"T-complex protein 1 subunit delta":195,"T-complex protein 1 subunit eta":195,"T-complex protein 1 subunit theta":195,"T-complex protein 1 subunit zeta":195,"UGDH":195,"VCP":195,"Yersinia":195,"alpha-galactosidase activity":195,"axon extension involved in axon guidance":195,"cellular response to caffeine":195,"cholesterol transport":195,"hpcd":195,"insulin-like growth factor-activated receptor activity":195,"lipopolysaccharide core region biosynthetic process":195,"mismatch repair complex":195,"myoblast fusion":195,"negative regulation of focal adhesion assembly":195,"nuclear import":195,"pcaH":195,"protein maturation":195,"regulation of osteoblast proliferation":195,"-!- This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen. -!- The reaction can be considered as the reverse of 'carbamate = cyanate + H(2)O', where this is assisted by reaction with bicarbonate and carbon dioxide, and hence is classified in sub-subclass 4.2.1. -!- Bicarbonate functions as a recycling substrate. -!- Formerly EC 3.5.5.3 and EC 4.3.99.1.":194,"ANC2, CCT4, TCP4, YDL143W":194,"Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446":194,"BIN2, CCT3, J1336, TCP3, YJL014W":194,"BIN3, CCT2, TCP2, YIL142W":194,"CCT1, TCP1, YD8142.13, YD8142B.04, YDR212W":194,"CCT5, J1752, TCP5, YJR064W":194,"CCT6, TCP20, TCP6, YD9395.21, YDR188W":194,"CCT7, J0804, YJL111W":194,"CCT8, J1374, YJL008C":194,"Cyanase.":194,"Cyanate + HCO(3)(-) + 2 H(+) = NH(3) + 2 CO(2).":194,"Cyanate aminohydrolase. Cyanate C-N-lyase. Cyanate hydratase. Cyanate hydrolase. Cyanate lyase.":194,"Cyanate hydratase":194,"Human poliovirus 1 Mahoney":194,"Maltose/maltodextrin import ATP-binding protein MalK":194,"RISC-loading complex":194,"Rhodococcus opacus":194,"Slime mold":194,"T-complex protein 1 subunit epsilon":194,"adenyl-nucleotide exchange factor activity":194,"biotin binding":194,"chromatin silencing":194,"entry into host via enzymatic degradation of host anatomical structure":194,"extracellular-glutamate-gated ion channel activity":194,"histone H3-K79 methylation":194,"histone ubiquitination":194,"juxtaparanode region of axon":194,"kcsA, skc1":194,"keratin filament binding":194,"misfolded protein binding":194,"necroptotic process":194,"protein demethylation":194,"protein neddylation":194,"pyruvate dehydrogenase activity":194,"regulation of establishment of protein localization to plasma membrane":194,"vitamin D receptor binding":194,"2-HYDROXYBENZOIC ACID":193,"4'-HYDROXYCINNAMIC ACID":193,"ADP-ribosyl cyclase 1":193,"Calmodulin 2":193,"Catechol O-methyltransferase":193,"DNA repair and recombination protein RadA":193,"Ribosomal protein uL2":193,"Superoxide dismutase [Mn], mitochondrial":193,"Synechococcus sp.":193,"Ubiquinol-cytochrome c reductase iron-sulfur subunit":193,"YTTRIUM (III) ION":193,"abscisic acid-activated signaling pathway":193,"carbon monoxide binding":193,"catechol O-methyltransferase activity":193,"ionotropic glutamate receptor binding":193,"keratan sulfate catabolic process":193,"oligodendrocyte differentiation":193,"pH-gated potassium channel KcsA":193,"positive regulation of ATPase activity":193,"positive regulation of glucose import in response to insulin stimulus":193,"response to hormone":193,"response to vitamin A":193,"toxin":193,"ubiquitin-like protein conjugating enzyme binding":193,"viral budding from ER membrane":193,"viral envelope":193,"-!- Highly specific.":192,"-!- Menaquinone or other quinones can act as acceptor. -!- Inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. -!- Formerly EC 1.6.99.5.":192,"-!- The enzyme catalyzes the terminal step in the heme biosynthesis pathways of eukaryotes and Gram-negative bacteria.":192,"10-PROPARGYL-5,8-DIDEAZAFOLIC ACID":192,"180-meric":192,"60S ribosomal protein L37-A":192,"ATP-dependent protease ATPase subunit HslU":192,"Ferrochelatase. Heme synthase. Iron chelatase. Protoheme ferro-lyase.":192,"HEPTYL 1-THIOHEXOPYRANOSIDE":192,"INTEGRIN BETA-3":192,"Macaca mulatta polyomavirus 1":192,"Mahoney":192,"NADH + a quinone = NAD(+) + a quinol.":192,"NADH dehydrogenase (quinone).":192,"NuA4 histone acetyltransferase complex":192,"Peptidoglycan recognition protein 1":192,"Protein hfq":192,"Protoheme + 2 H(+) = protoporphyrin + Fe(2+).":192,"Protoporphyrin ferrochelatase.":192,"Ribosomal protein uL12":192,"SERRATIA MARCESCENS":192,"Spinacia":192,"Squalus acanthias":192,"Transcriptional regulator (NtrC family)":192,"action potential":192,"cAMP-mediated signaling":192,"cell-cell junction organization":192,"coenzyme-B sulfoethylthiotransferase activity":192,"nitrogen compound metabolic process":192,"nucleoside-triphosphatase activity":192,"positive regulation of endoplasmic reticulum unfolded protein response":192,"positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway":192,"regulation of cohesin loading":192,"spinach":192,"-!- Many enzymes previously listed under this number are now listed separately as EC 3.6.1.32 to EC 3.6.1.39. -!- The remaining enzymes, not separately listed on the basis of some function coupled with hydrolyzes of ATP, include enzymes dependent on Ca(2+), Mg(2+), anions, H(+) or DNA. -!- Formerly EC 3.6.1.4.":191,"-!- The enzyme catalyzes hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. -!- Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.":191,"-!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69.":191,"60S ribosomal protein L15-A":191,"60S ribosomal protein L17-A":191,"60S ribosomal protein L21-A":191,"60S ribosomal protein L26-A":191,"60S ribosomal protein L7-A":191,"60S ribosomal protein L8-A":191,"ACETYLCHOLINE BINDING PROTEIN":191,"Adenosinetriphosphatase.":191,"Adenylpyrophosphatase. ATP monophosphatase. ATPase. Triphosphatase.":191,"Alpha-D-xyloside xylohydrolase.":191,"Alpha-xylosidase.":191,"Bacteroides ovatus":191,"CYCLIN-DEPENDENT KINASE 2":191,"Cell division protein FtsZ":191,"DNA polymerase III subunit tau":191,"DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7":191,"Dda3937_00520":191,"GENE REGULATION/DNA":191,"Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.":191,"If kappa light chain":191,"MHC class II protein binding":191,"Neurospora crassa":191,"Photosystem II reaction center protein I":191,"Photosystem II reaction center protein L":191,"Photosystem II reaction center protein T":191,"R-47":191,"RNA (119-MER)":191,"RNA (2848-MER)":191,"SUGAR (N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE)":191,"TRANSFERASE/DNA/RNA":191,"U1 small nuclear ribonucleoprotein A":191,"UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase":191,"XANTHINE DEHYDROGENASE":191,"cobalamin transport":191,"dystroglycan binding":191,"heart looping":191,"lipopolysaccharide biosynthetic process":191,"mouse-ear cress, thale-cress":191,"negative regulation of bicellular tight junction assembly":191,"negative regulation of intracellular estrogen receptor signaling pathway":191,"negative regulation of myosin-light-chain-phosphatase activity":191,"protein maturation by protein folding":191,"rRNA binding":191,"regulation of nitrogen utilization":191,"sulfur amino acid metabolic process":191,"tRNA-Met":191,"termination of RNA polymerase I transcription":191,"2308":190,"60S ribosomal protein L31-A":190,"60S ribosomal protein L4-A":190,"60S ribosomal protein L9-A":190,"70S, Ribosome, Dityromycin, GE82832, Ribosomal Protein S12, EF-G, Translocation, Dityromycin and GE82832 bind protein S12 and block EF-G catalyzed translocation, 30S subunit with bound mRNA, P-site tRNA, Ribosome-Antibiotic complex":190,"Classic Zinc Finger":190,"DNA (5'-D(*CP*TP*GP*CP*TP*TP*AP*TP*CP*GP*GP*TP*AP*G)-3')":190,"HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN":190,"LISTERIA MONOCYTOGENES":190,"Mycobacterium avium 104":190,"Neutrophil gelatinase-associated lipocalin":190,"S-6":190,"Solanum tuberosum":190,"Thermoactinomyces":190,"chromatin-mediated maintenance of transcription":190,"collateral sprouting":190,"cow":190,"exo-alpha-sialidase activity":190,"forebrain development":190,"germ cell development":190,"glucose-6-phosphate isomerase activity":190,"negative regulation of phosphorylation":190,"negative regulation of protein localization to cell surface":190,"nucleosomal DNA binding":190,"oxidoreductase/oxidoreductase inhibitor":190,"positive regulation of fat cell differentiation":190,"protein K48-linked deubiquitination":190,"protein localization to synapse":190,"receptor agonist activity":190,"60S ribosomal protein L14-A":189,"60S ribosomal protein L24-A":189,"60S ribosomal protein L6-A":189,"ALPHA-D-GLUCOSE":189,"ATP1, YBL099W, YBL0827":189,"ATP15, YPL271W, P0345":189,"ATP16, YDL004W, YD8119.03, D2935":189,"ATP2, YJR121W, J2041":189,"Bordetella":189,"C-125":189,"Desulfovibrio vulgaris str. 'Miyazaki F'":189,"Nuclear receptor coactivator 1":189,"PACTAMYCIN":189,"SYNTHASE":189,"Unp residues 10-1024":189,"Xanthomonas":189,"androgen receptor activity":189,"cardiac muscle tissue morphogenesis":189,"cellular bud neck":189,"endocrine pancreas development":189,"hair follicle development":189,"long-chain fatty acid binding":189,"negative regulation by host of viral transcription":189,"odontogenesis":189,"positive regulation of dendritic spine development":189,"positive regulation of smooth muscle cell migration":189,"positive regulation of transcription from RNA polymerase II promoter in response to hypoxia":189,"protein metabolic process":189,"rRNA base methylation":189,"regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling":189,"skeletal muscle thin filament assembly":189,"-!- Catalyzes template-independent extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Nucleoside may be ribo- or deoxyribo-.":188,"-!- Converts a wide range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes. -!- The allyl group of 4-allylphenols is also converted into the -CH=CH-CH(2)OH group.":188,"3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE":188,"4-hydroxy-2-methoxybenzyl alcohol oxidase.":188,"ATP SYNTHASE, ATP PHOSPHATASE, F1F0 ATPASE, ATP SYNTHESIS, HYDROLASE, ADP, PO4, MITOCHONDRIA":188,"Amycolatopsis orientalis":188,"BACTERIOPHEOPHYTIN B":188,"Chitinase-3-like protein 1":188,"Cytochrome b-large subunit":188,"DNA nucleotidylexotransferase":188,"DNA nucleotidylexotransferase activity":188,"DNA nucleotidylexotransferase.":188,"DNA polymerase processivity factor activity":188,"DNA topoisomerase complex (ATP-hydrolyzing)":188,"ENDONUCLEASE":188,"Klebsiella pneumoniae subsp. pneumoniae":188,"Magnaporthe oryzae 70-15":188,"SERINE HYDROXYMETHYLTRANSFERASE":188,"Sec61 alpha subunit":188,"Sec61 beta subunit":188,"Sec61 gamma subunit":188,"THROMBIN HEAVY CHAIN":188,"Terminal addition enzyme. Terminal deoxynucleotidyltransferase. Terminal deoxyribonucleotidyltransferase. Terminal transferase.":188,"Vanillyl alcohol + O(2) = vanillin + H(2)O(2).":188,"Vanillyl-alcohol oxidase.":188,"Vascular endothelial growth factor receptor 2":188,"adenosylmethionine-8-amino-7-oxononanoate transaminase activity":188,"brain":188,"cellular response to fructose stimulus":188,"dTMP biosynthetic process":188,"dihydroorotate dehydrogenase activity":188,"interaction with other organism via secreted substance involved in symbiotic interaction":188,"lipid transport":188,"membrane protein intracellular domain proteolysis":188,"negative regulation of smooth muscle cell migration":188,"neuromuscular junction development":188,"regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion":188,"release of sequestered calcium ion into cytosol by sarcoplasmic reticulum":188,"tyrosine catabolic process":188,"-!- Requires calmodulin. -!- A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light-chains and the microtubule- associated tau protein. -!- Not identical with EC EC 2.7.11.18 or EC 2.7.11.26. -!- Formerly EC 2.7.1.120 and EC 2.7.1.123.":187,"1,4-beta-cellobiohydrolase. 4-beta-D-glucan cellobiohydrolase (non-reducing end). Avicelase. Exo-1,4-beta-D-glucanase. Exocellobiohydrolase. Exoglucanase.":187,"ATCC 51907 / DSM 11121 / KW20 / Rd":187,"Acyl carrier protein":187,"CYTOCHROME C OXIDASE":187,"Ca(2+)/calmodulin-dependent microtubule-associated protein 2 kinase. Ca(2+)/calmodulin-dependent protein kinase 1. Ca(2+)/calmodulin-dependent protein kinase II. Ca(2+)/calmodulin-dependent protein kinase IV. Ca(2+)/calmodulin-dependent protein kinase kinase. Ca(2+)/calmodulin-dependent protein kinase kinase beta. Calcium/calmodulin-dependent protein kinase type II. Caldesmon kinase. Caldesmon kinase (phosphorylating). Calmodulin-dependent kinase II. CaM kinase. CaM kinase II. CAM PKII. CaM-regulated serine/threonine kinase. CaMKI. CaMKII. CaMKIV. CaMKK-alpha. CaMKK-beta. Microtubule-associated protein 2 kinase.":187,"Calcium/calmodulin-dependent protein kinase.":187,"Cellulose 1,4-beta-cellobiosidase (non-reducing end).":187,"Citrobacter freundii":187,"Cul2-RING ubiquitin ligase complex":187,"DIMETHYLFORMAMIDE":187,"Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.":187,"MOZ/MORF histone acetyltransferase complex":187,"Nitrogenase iron protein 1":187,"RNA polymerase II, initiation complex, TRANSCRIPTION-RNA-DNA complex":187,"TRANSFERASE/TRANSFERASE inhibitor":187,"cellular response to gonadotropin stimulus":187,"cyanate catabolic process":187,"glutamate receptor signaling pathway":187,"medium-chain fatty acid metabolic process":187,"mercury ion binding":187,"phosphothreonine binding":187,"positive regulation of actin nucleation":187,"positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway":187,"proteasome binding":187,"smoothened signaling pathway":187,"-!- Occurs as a tetrameric molecule with high affinity for heparin, in mast cell granules. -!- Not inhibited by alpha-1-proteinase inhibitor of alpha-2- macroglobulin. -!- Belongs to peptidase family S1.":186,"-!- The product decarboxylates to 5-hydroxy-4-oxopentanoate. -!- The enzyme can decarboxylate 2-oxoglutarate. -!- Acetaldehyde can replace glyoxylate. -!- Formerly EC 4.1.3.15.":186,"2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating). 2-hydroxy-3-oxoadipate synthetase. Alpha-ketoglutaric-glyoxylic carboligase. Oxoglutarate: glyoxylate carboligase.":186,"2-hydroxy-3-oxoadipate synthase.":186,"2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2).":186,"2-oxoglutarate = succinate semialdehyde + CO(2).":186,"2-oxoglutarate carboxy-lyase. Alpha-ketoglutarate decarboxylase.":186,"2-oxoglutarate decarboxylase.":186,"5":186,"Cobalt/magnesium transport protein CorA":186,"Deoxynucleoside triphosphate triphosphohydrolase SAMHD1":186,"KANAMYCIN A":186,"Lung tryptase. Mast cell protease II. Mast cell tryptase. Pituitary tryptase. Skin tryptase.":186,"MENAQUINONE-7":186,"Multifunctional 2-oxoglutarate metabolism enzyme":186,"PIG":186,"Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.":186,"RIG-I signaling pathway":186,"Triphosphoric monoester hydrolases.":186,"Tryptase.":186,"alkaline phosphatase activity":186,"dUTP diphosphatase activity":186,"hemi-methylated DNA-binding":186,"house mouse, human":186,"negative regulation of T cell receptor signaling pathway":186,"negative regulation of dendritic spine maintenance":186,"positive regulation of superoxide dismutase activity":186,"3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL":185,"ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.":185,"DNA-directed RNA polymerase subunit L":185,"ERYTHROMYCIN A":185,"Galactose-binding domain-like":185,"HYDROLASE, SINGLE-PARTICLE, P97, AAA ATPASE":185,"IRE1-TRAF2-ASK1 complex":185,"NS3":185,"OXIDOREDUCTASE/TRANSFERASE":185,"RNA polymerase II carboxy-terminal domain kinase activity":185,"Succinate thiokinase. Succinyl-CoA synthetase (ADP-forming).":185,"Succinate--CoA ligase (ADP-forming).":185,"Superoxide dismutase":185,"THROMBIN LIGHT CHAIN":185,"THYMIDINE":185,"TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE":185,"VALINE":185,"astral microtubule organization":185,"hydro-lyase activity":185,"magnesium ion transmembrane transporter activity":185,"mitogen-activated protein kinase kinase kinase binding":185,"negative regulation of insulin receptor signaling pathway":185,"negative regulation of protein processing":185,"plasma membrane fumarate reductase complex":185,"positive regulation of keratinocyte differentiation":185,"positive regulation of protein localization to early endosome":185,"protein antigen binding":185,"structural constituent of eye lens":185,"type II transforming growth factor beta receptor binding":185,"-!- A group of enzymes found in invertebrates and microorganisms highly specific for glucose.":184,"-!- The enzyme from heart mitochondria is Re-specific with respect to NAD(+) and Si-specific with respect to NADP(+) (cf. EC 1.6.1.1.).":184,"ACETYLCHOLINE-BINDING PROTEIN":184,"AMINE OXIDASE [FLAVIN-CONTAINING] B":184,"ATP + D-glucose = ADP + D-glucose 6-phosphate.":184,"CVT pathway":184,"General control protein GCN4":184,"Glucokinase.":184,"Glucose kinase.":184,"Influenza B virus":184,"NAD(P)(+) transhydrogenase (AB-specific). Pyridine nucleotide transhydrogenase. Transhydrogenase.":184,"NAD(P)(+) transhydrogenase (Re/Si-specific).":184,"NADPH + NAD(+) = NADP(+) + NADH.":184,"NF-kappaB-inducing kinase activity":184,"REPLICATION/DNA":184,"RNA polymerase II repressing transcription factor binding":184,"Staphylococcus aureus subsp. aureus str. Newman":184,"Thymidylate synthase thyX":184,"UNP residues 49-189":184,"autophagosome membrane":184,"cellular response to hydroperoxide":184,"fatty acid synthase complex":184,"hair follicle morphogenesis":184,"membrane to membrane docking":184,"microtubule associated complex":184,"mitophagy":184,"positive regulation of integrin activation":184,"positive regulation of type I hypersensitivity":184,"positive regulation of type IIa hypersensitivity":184,"regulation of establishment of cell polarity":184,"rhythmic process":184,"short-term memory":184,"single-stranded telomeric DNA binding":184,"-!- Formerly EC 6.3.1.3.":183,"ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase":183,"ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)- (5-phospho-D-ribosyl)glycinamide.":183,"CDNA":183,"DNA PROTECTION DURING STARVATION PROTEIN":183,"GAR synthetase. GARS. Glycinamide ribonucleotide synthetase. Phosphoribosylglycinamide synthetase.":183,"INTEGRIN ALPHA-IIB":183,"MDM2":183,"Methionine aminopeptidase":183,"Phosphoribosylamine--glycine ligase.":183,"Ribosome inactivating protein":183,"SALMONELLA TYPHIMURIUM":183,"SFVcpz(hu)":183,"TANKYRASE-2":183,"UDP-GlcNAc 4-epimerase. Uridine diphosphoacetylglucosamine epimerase.":183,"UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine.":183,"UDP-N-acetylglucosamine 4-epimerase.":183,"UNDECANE":183,"biosynthesis by symbiont of substance in host":183,"calcium- and calmodulin-responsive adenylate cyclase activity":183,"common tobacco":183,"fibrinogen binding":183,"lung alveolus development":183,"macrolide biosynthetic process":183,"negative regulation of protein export from nucleus":183,"phosphodiesterase I activity":183,"positive regulation of Rho protein signal transduction":183,"pyrimidine nucleoside catabolic process":183,"(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.":182,"-!- Also catalyzes the interconversion of 3-acetylenic fatty acyl thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty acid chain lengths C(6) to C(12).":182,"3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase.":182,"3-phosphoshikimate 1-carboxyvinyltransferase":182,"70S, ribosome, IGR, IRES, PSIV, CrPV":182,"Cytophaga hutchinsonii ATCC 33406":182,"DSM 1495 / CBS 144.50 / IMI 039719":182,"Dodecenoyl-CoA isomerase.":182,"Eight-heme nitrite reductase":182,"PROTOCATECHUATE 3,4-DIOXYGENASE":182,"PYRUVATE KINASE":182,"Photosynthetic reaction center cytochrome c subunit":182,"STRUCTURAL GENOMICS":182,"Salmonella phage HK620":182,"UNP RESIDUES 297-718":182,"UNP residues 20-241":182,"erythrocyte homeostasis":182,"establishment of protein localization to mitochondrion":182,"glr4197":182,"glycerol biosynthetic process from pyruvate":182,"maintenance of protein location in mitochondrion":182,"nicotinate-nucleotide diphosphorylase (carboxylating) activity":182,"nitric oxide catabolic process":182,"phosphoenolpyruvate carboxykinase activity":182,"proline catabolic process":182,"regulation of mitotic cell cycle phase transition":182,"response to methionine":182,"ribonucleoprotein complex binding":182,"-!- Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. -!- May be identical to EC 1.7.2.1.":181,"ACHROMOBACTER XYLOSOXIDANS":181,"CREB-binding protein":181,"DODECYL-ALPHA-D-MALTOSIDE":181,"ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADPH]":181,"Fab Light Chain":181,"Hydroxylamine (acceptor) reductase.":181,"Hydroxylamine reductase.":181,"L-serine biosynthetic process":181,"NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor.":181,"Protease degS":181,"RNA secondary structure unwinding":181,"Sphingomonas paucimobilis":181,"U2-type prespliceosome":181,"dihydrofolic acid binding":181,"glutathione-disulfide reductase activity":181,"mitochondrial fragmentation involved in apoptotic process":181,"neuroligin family protein binding":181,"pcaG":181,"positive regulation of histone H3-K4 methylation":181,"spermatid development":181,"transcription elongation from RNA polymerase I promoter":181,"(4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE":180,"204508":180,"CAMPHOR":180,"CDC 1551 / Oshkosh":180,"Capsid":180,"DSM 12444":180,"E3 ubiquitin-protein ligase XIAP":180,"HEXANE":180,"Lysobacter enzymogenes":180,"MDM2/MDM4 family protein binding":180,"Medicago":180,"Methyltransferase":180,"Momordica balsamina":180,"PHOSPHOLIPASE A2":180,"Potassium Channel Kv1.1; Chain A":180,"RESIDUES 26-297":180,"Rattus rattus":180,"SCHU S4":180,"adenosylhomocysteinase activity":180,"adenylate cyclase-modulating G-protein coupled receptor signaling pathway":180,"cGMP binding":180,"cardiac muscle fiber development":180,"copper ion homeostasis":180,"histone H3 deacetylation":180,"multicellular organismal reproductive process":180,"negative regulation of execution phase of apoptosis":180,"pilus":180,"recombinational repair":180,"regulation of caveolin-mediated endocytosis":180,"regulation of neurogenesis":180,"sodium channel inhibitor activity":180,"transfer RNA":180,"-!- Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.":179,"-!- The reaction shown is in the pathway of biosynthesis of valine. -!- The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine. -!- Formerly EC 4.1.3.18.":179,"-!- This enzyme, found in carboxydotrophic bacteria, catalyzes the oxidation of CO to CO(2) under aerobic conditions. -!- The enzyme belongs to the xanthine oxidoreductase family. -!- The CO(2) that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor. -!- Cf. EC 1.2.7.4.":179,"11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity":179,"2 pyruvate = 2-acetolactate + CO(2).":179,"ARTIFICIAL GENE":179,"Acetohydroxy acid synthetase. Acetohydroxyacid synthase. Acetolactate pyruvate-lyase (carboxylating). Acetolactic synthetase. Alpha-acetohydroxy acid synthetase. Alpha-acetohydroxyacid synthase. Alpha-acetolactate synthase. Alpha-acetolactate synthetase.":179,"Acetolactate synthase.":179,"Aerobic carbon monoxide dehydrogenase.":179,"CO + a quinone + H(2)O = CO(2) + a quinol.":179,"DNA (25-MER)":179,"Enterobacteria phage P22":179,"Ferritin light chain":179,"HEAVY CHAIN":179,"HIV-1 POL":179,"Human rhinovirus B14":179,"IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.":179,"IMP cyclohydrolase.":179,"IMP synthetase. Inosinicase.":179,"L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H.":179,"MW2":179,"Molybdoenzyme carbon monoxide dehydrogenase.":179,"NAD(P)H oxidase activity":179,"P-HYDROXYBENZOIC ACID":179,"P5CR.":179,"PROTEASE":179,"Protective antigen":179,"Protein biosynthesis, ribosome, RNA, tRNA, transfer RNA, 30S, 70S, 16S, 23S, ribosomal subunit":179,"Pyrroline-5-carboxylate reductase.":179,"RIBONUCLEASE A":179,"RUBIDIUM ION":179,"S-HEXYLGLUTATHIONE":179,"SNRPF, PBSCF":179,"SNRPG, PBSCG":179,"SPERMINE":179,"alpha-tubulin binding":179,"associative learning":179,"cellular heat acclimation":179,"definitive hemopoiesis":179,"detection of muscle stretch":179,"eukaryotic translation initiation factor 4F complex":179,"flavonoid metabolic process":179,"flotillin complex":179,"negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway":179,"neuron cell-cell adhesion":179,"positive regulation by host of viral transcription":179,"positive regulation of mitochondrial depolarization":179,"pyridoxine biosynthetic process":179,"regulation of growth plate cartilage chondrocyte proliferation":179,"regulation of vesicle-mediated transport":179,"response to fungus":179,"response to interferon-gamma":179,"-!- The enzyme catalyzes a committed step in the biosynthesis of lipid A. -!- Formerly EC 3.5.1.n1.":178,"-!- The enzyme catalyzes the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. -!- Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO(2). -!- Formerly EC 4.1.3.2.":178,"ATF6-mediated unfolded protein response":178,"ATP synthase epsilon chain":178,"Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA.":178,"COMPLEMENT C3 BETA CHAIN":178,"Cul4-RING E3 ubiquitin ligase complex":178,"Cytochrome c peroxidase":178,"FAB HEAVY CHAIN":178,"FAB LIGHT CHAIN":178,"Glucocorticoid receptor":178,"Glyoxylate transacetase. Glyoxylate transacetylase. Glyoxylic transacetase. L-malate glyoxylate-lyase (CoA-acetylating). Malate condensing enzyme. Malate synthetase. Malic synthetase. Malic-condensing enzyme.":178,"H(+)/Cl(-) exchange transporter clcA":178,"HEME DOMAIN":178,"Human immunodeficiency virus type 1 (BH5 ISOLATE)":178,"Malate synthase.":178,"PSEUDOMONAS AERUGINOSA PAO1":178,"Protein FimH":178,"Rhinovirus":178,"S-adenosylmethionine biosynthetic process":178,"SUGAR (ALPHA-D-GLUCOSE-6-PHOSPHATE)":178,"UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + acetate.":178,"UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. UDP-3-O-(3-hydroxymyristoyl) N-acetylglucosamine deacetylase. UDP-3-O-acyl-GlcNAc deacetylase.":178,"UDP-3-O-acyl-N-acetylglucosamine deacetylase":178,"UDP-3-O-acyl-N-acetylglucosamine deacetylase.":178,"apolipoprotein A-I receptor binding":178,"axon guidance receptor activity":178,"horse":178,"negative regulation of lipid catabolic process":178,"positive regulation of lipid biosynthetic process":178,"rRNA methylation":178,"rpll":178,"steroid hydroxylase activity":178,"(1) Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). (2) Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+).":177,"(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase. HMBPP reductase.":177,"-!- Dihtheria toxin and some other bacterial toxins catalyze this reaction, which inactivates translation elongation factor 2 (EF2). -!- The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. -!- Cf. EC 2.4.2.31. -!- The relevant histidine of EF2 is His(715) in mammals, His(699) in yeast and His(600) in Pyrococcus horikoshii.":177,"-!- Forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. -!- This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. -!- This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. -!- The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate. -!- Formerly EC 1.17.1.2.":177,"4-hydroxy-3-methylbut-2-enyl diphosphate reductase.":177,"ADP-ribosyltransferase. Mono(ADP-ribosyl)transferase.":177,"Actin-related protein 3":177,"Bacteriophytochrome":177,"D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE":177,"D-serine metabolic process":177,"Mannose PTS permease.":177,"Mus, Homo":177,"NAD(+) + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2].":177,"NAD(+)--diphthamide ADP-ribosyltransferase.":177,"O-GlcNAcase BT_4395":177,"Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1":177,"Proline--tRNA ligase":177,"Protein-N(pi)-phosphohistidine--D-mannose phosphotransferase.":177,"SUPEROXIDE DISMUTASE":177,"Simian virus 40":177,"Tyrosine-protein kinase ITK/TSK":177,"[Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L- histidine + D-mannose 6-phosphate(Side 2).":177,"black rat":177,"double-stranded telomeric DNA binding":177,"glutaminase activity":177,"negative regulation of pinocytosis":177,"negative regulation of sodium ion transmembrane transporter activity":177,"oxysterol binding":177,"phosphatidylcholine catabolic process":177,"phosphoglucomutase activity":177,"pyoverdine biosynthetic process":177,"regulation of pathway-restricted SMAD protein phosphorylation":177,"response to muramyl dipeptide":177,"striated muscle cell differentiation":177,"suppression by virus of host transcription":177,"voltage-gated calcium channel activity":177,"-!- A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta- substituted alpha-L-amino acids and a variety of mercaptans. -!- Formerly EC 4.2.1.21.":176,"2-phospho-D-glycerate = 3-phospho-D-glycerate.":176,"BIOSYNTHETIC PROTEIN/TRANSFERASE":176,"Beta-thionase. Methylcysteine synthase. Serine sulfhydrase.":176,"Biphenyl dioxygenase subunit alpha":176,"Cystathionine beta-synthase.":176,"DNA gyrase subunit A":176,"Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774":176,"GLUTAMATE RECEPTOR 2":176,"Giardia intestinalis":176,"Hematopoietic prostaglandin D synthase":176,"Integrin alpha-L":176,"L-serine + L-homocysteine = L-cystathionine + H(2)O.":176,"L-serine metabolic process":176,"OXIDOREDUCTASE, TRANSFERASE":176,"PROTON TRANSPORT":176,"Photosystem II D2 protein":176,"VHL":176,"developmental process":176,"endopeptidase inhibitor activity":176,"inorganic diphosphatase activity":176,"iron-sulfur cluster assembly":176,"lipoxygenase pathway":176,"microtubule nucleation":176,"motor neuron axon guidance":176,"mthK, MTH_1520":176,"protein targeting to Golgi":176,"siRNA loading onto RISC involved in RNA interference":176,"skeletal muscle myosin thick filament assembly":176,"(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH.":175,"-!- The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi- functional protein complex composed of two subunits. -!- One subunit catalyzes the reactions EC 1.1.1.100 and EC 2.3.1.41, while the other subunit catalyzes the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 4.2.1.59, EC 1.3.1.10 and EC 1.1.1.279. -!- The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.":175,"3-isopropylmalate dehydrogenase.":175,"Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).":175,"Beta-IPM dehydrogenase. Beta-isopropylmalate dehydrogenase. IMDH.":175,"Colwellia psychrerythraea 34H":175,"Complement factor H":175,"Cytochrome b-c1 complex subunit 2, mitochondrial":175,"D-ALANYL-D-ALANINE CARBOXYPEPTIDASE":175,"Distal tail protein, Receptor-binding protein, Phage baseplate, host adsorption apparatus, genome injection device, VIRAL PROTEIN":175,"ESCHERICHIA COLI K-12":175,"F11":175,"Fatty-acyl-CoA synthase.":175,"G-protein alpha-subunit binding":175,"GLYCOSYLTRANSFERASE":175,"GUANINE":175,"Listeria":175,"Methionine--tRNA ligase":175,"NITRIC OXIDE SYNTHASE OXYGENASE":175,"Post-decarboxylation intermediate, TRANSFERASE":175,"SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT":175,"Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH.":175,"Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase.":175,"UNP residues 84-605":175,"Urease subunit alpha":175,"Yeast fatty acid synthase.":175,"cytoplasmic microtubule organization":175,"dendritic cell differentiation":175,"menD, b2264, JW5374":175,"negative regulation of interleukin-6-mediated signaling pathway":175,"negative regulation of plasma membrane long-chain fatty acid transport":175,"positive regulation of T cell chemotaxis":175,"rRNA transcription":175,"receptor-mediated virion attachment to host cell":175,"regulation of cGMP metabolic process":175,"regulation of endopeptidase activity":175,"-!- Catalyzes the activation of molybdopterin for molybdenum insertion. -!- In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1). -!- The reaction requires a divalent cation such as Mg(2+) or Mn(2+). -!- Catalyzes the activation of molybdopterin for molybdenum insertion. -!- In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes EC 2.10.1.1. -!- Formerly EC 2.7.7.n5.":174,"1,4-BUTANEDIOL":174,"2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID":174,"3,5,7,3',4'-PENTAHYDROXYFLAVONE":174,"ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.":174,"Ac-PAE-ep":174,"BALB/C":174,"Brucella abortus":174,"Cysteine synthase":174,"Cytochrome b-c1 complex subunit 1, mitochondrial":174,"Desulfovibrio africanus":174,"E3 ubiquitin-protein ligase CBL":174,"Erwinia chrysanthemi":174,"Guanyl-specific ribonuclease T1":174,"HEAT SHOCK PROTEIN HSP 90-ALPHA":174,"MAP kinase kinase kinase activity":174,"Molybdopterin adenylyltransferase.":174,"PROTEASOME SUBUNIT BETA TYPE-5":174,"Paramecium bursaria Chlorella virus 1":174,"Phospholipase A2":174,"Putative lipoprotein":174,"Threonine--tRNA ligase":174,"UNP residues 20-215":174,"UNP residues 76-287":174,"actin cap":174,"aggregation involved in sorocarp development":174,"carboxy-lyase activity":174,"cellular response to dsRNA":174,"dopamine biosynthetic process":174,"interleukin-6 receptor binding":174,"internal protein amino acid acetylation":174,"lithocholic acid binding":174,"negative regulation of interleukin-10 production":174,"negative regulation of protein homodimerization activity":174,"negative regulation of protein sumoylation":174,"piecemeal microautophagy of nucleus":174,"positive regulation of cell-cell adhesion":174,"positive regulation of protein kinase C signaling":174,"protein localization to Golgi apparatus":174,"regulation of T cell proliferation":174,"regulation of transcription from RNA polymerase III promoter":174,"telethonin binding":174,"virus attachment, membrane fusion, VIRAL PROTEIN":174,"1,3-DIHYDROXYACETONEPHOSPHATE":173,"2":173,"ARSENIC":173,"ATP-dependent protein binding":173,"C-terminal protein lipidation":173,"Csal_2974":173,"DNA (145-MER)":173,"Enterococcus hirae ATCC 9790":173,"F7":173,"Galactose-binding lectin":173,"Insulin A chain":173,"Insulin B chain":173,"Leucine--tRNA ligase":173,"Lysine--tRNA ligase":173,"PEPTIDE":173,"PTERIN CYTOSINE DINUCLEOTIDE":173,"Phosphopantetheine adenylyltransferase":173,"Photosystem Q(B) protein":173,"Polyomavirus":173,"Rhodobacter capsulatus SB 1003":173,"Toxoplasma gondii VEG":173,"[[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-TRIS(FLUORANYL)BERYLLIUM":173,"apoptotic mitochondrial changes":173,"bent DNA binding":173,"cyanate hydratase activity":173,"embryonic hemopoiesis":173,"face morphogenesis":173,"intracellular receptor signaling pathway":173,"negative regulation of monocyte differentiation":173,"negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels":173,"pantoate-beta-alanine ligase activity":173,"-!- Also acts on acyl and choline analogs.":172,"1-alkyl-sn-glycero-3-phosphoethanolamine + H(2)O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine.":172,"60S ribosomal protein L11-A":172,"A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-oxosteroid + NAD(P)H.":172,"ADP1":172,"AMPA glutamate receptor clustering":172,"Alkylglycerophosphoethanolamine phosphodiesterase.":172,"BACTERIOCHLOROPHYLL B":172,"Cys-loop ligand-gated ion channel":172,"D-GLUTAMIC ACID":172,"Dihydroxyacetone transferase. Glycerone transferase.":172,"Ectonucleotide pyrophosphatase/phosphodiesterase family member 2":172,"Endo-1,4-beta-xylanase A":172,"Enterobacteria phage P1":172,"Glucanase":172,"HLA class I histocompatibility antigen, A-24 alpha chain":172,"HYDROLASE/PEPTIDE":172,"Insulin":172,"Lysophospholipase D.":172,"Primary amine oxidase":172,"Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.":172,"Thioalkalivibrio nitratireducens DSM 14787":172,"Transaldolase.":172,"UNP residues 25-298":172,"ammonium ion metabolic process":172,"border follicle cell migration":172,"cAMP-specific 3',5'-cyclic phosphodiesterase 4D":172,"cardiac myofibril assembly":172,"endomembrane system":172,"glutathione biosynthetic process":172,"hyphal tip":172,"ligase/ligase inhibitor":172,"negative regulation of renal sodium excretion":172,"negative regulation of toll-like receptor 4 signaling pathway":172,"sarcomerogenesis":172,"uropod":172,"-!- Activity is dependent on a redox-active disulfide in each of the active centers. -!- Formerly EC 1.6.4.2.":171,"1a":171,"2 glutathione + NADP(+) = glutathione disulfide + NADPH.":171,"ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM":171,"ATP SYNTHASE SUBUNIT BETA":171,"Alpha-amylase":171,"Artocarpus integer":171,"CISPLATIN":171,"Capra hircus":171,"Glutathione reductase. Glutathione reductase (NADPH). Glutathione S-reductase. GSH reductase. GSSG reductase. NADPH-glutathione reductase. NADPH-GSSG reductase. NADPH:oxidized-glutathione oxidoreductase.":171,"Glutathione-disulfide reductase.":171,"HEMOGLOBIN MUTANT, GLOBIN, TRANSPORT PROTEIN":171,"Histone deacetylase 8":171,"Janthinobacterium sp. J3":171,"Lyme disease spirochete":171,"Medicago sativa":171,"Methane monooxygenase component A alpha chain":171,"Methane monooxygenase component A beta chain":171,"Mycoplasma":171,"NEDD8":171,"Pichia angusta":171,"Propionibacterium freudenreichii subsp. shermanii":171,"RESIDUES 44-553":171,"SF2":171,"STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PSI-2, Protein Structure Initiative, New York SGX Research Center for Structural Genomics, NYSGXRC":171,"Salmonella enterica subsp. enterica serovar Typhi":171,"TREHALOSE":171,"Transcriptional regulator":171,"ZEBRAFISH":171,"epithelial cell-cell adhesion":171,"interleukin-15-mediated signaling pathway":171,"nitrate reductase activity":171,"peptide":171,"peptidyl-methionine modification":171,"polyamine metabolic process":171,"response to herbicide":171,"(1) S-adenosyl-L-homocysteine + H(2)O = S-(5-deoxy-D-ribos-5-yl)-L- homocysteine + adenine. (2) S-methyl-5'-thioadenosine + H(2)O = 5-methyl-5-thio-D-ribose + adenine.":170,"(2S)-2-HYDROXYBUTANEDIOIC ACID":170,"-!- The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157.":170,"3'-dephospho-CoA pyrophosphorylase. Dephospho-CoA diphosphorylase. Dephospho-CoA pyrophosphorylase. Dephospho-coenzyme A pyrophosphorylase. Phosphopantetheine adenylyltransferase. PPAT.":170,"40S RIBOSOMAL PROTEIN S24":170,"40S RIBOSOMAL PROTEIN S6":170,"5'-methyladenosine nucleosidase. AdoHcy/MTA nucleosidase. S-adenosylhomocysteine hydrolase. S-adenosylhomocysteine nucleosidase. S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase.":170,"ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.":170,"Adenosylhomocysteine nucleosidase.":170,"Adenylosuccinate synthetase":170,"Alpha-lytic endopeptidase.":170,"Alpha-lytic protease":170,"Alpha-lytic protease.":170,"DIACYL GLYCEROL":170,"Mycobacterium avium":170,"N-(PHOSPHONACETYL)-L-ASPARTIC ACID":170,"Pantetheine-phosphate adenylyltransferase.":170,"Penicillium simplicissimum":170,"Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.":170,"Rubredoxin":170,"Succinate dehydrogenase flavoprotein subunit":170,"Thioredoxin reductase 1, cytoplasmic":170,"U6 snRNA binding":170,"UNP residues 19-147":170,"acyl-CoA dehydrogenase activity":170,"bacterial-type flagellum assembly":170,"cell projection membrane":170,"cellular process":170,"exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay":170,"hydroxymethylbutenyl pyrophosphate reductase activity":170,"leading edge membrane":170,"negative regulation of phosphoprotein phosphatase activity":170,"negative regulation of tyrosine phosphorylation of STAT protein":170,"positive regulation of norepinephrine secretion":170,"protein K63-linked deubiquitination":170,"residues 57-159":170,"1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE":169,"3-ketoacyl-CoA thiolase. Beta-ketothiolase.":169,"40S RIBOSOMAL PROTEIN S27":169,"40S RIBOSOMAL PROTEIN SA":169,"AZURIN":169,"Acetyl-CoA C-acyltransferase.":169,"Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.":169,"CHEK1, CHK1":169,"D-MALATE":169,"DNA-directed RNA polymerase subunit H":169,"Dihydrolipoyl dehydrogenase, mitochondrial":169,"Dual specificity protein kinase TTK":169,"Envelope glycoprotein":169,"Fluorescent protein Dronpa":169,"HIF hydroxylase.":169,"HSP90AA1, HSP90A, HSPC1, HSPCA":169,"J2315":169,"KINASE":169,"Legionella pneumophila subsp. pneumophila":169,"Methanosarcina acetivorans C2A":169,"NITRIC OXIDE SYNTHASE":169,"NMN diphosphorylase. NMN pyrophosphorylase.":169,"Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho- alpha-D-ribose 1-diphosphate.":169,"Nicotinamide phosphoribosyltransferase":169,"Nicotinamide phosphoribosyltransferase.":169,"Pig":169,"SAGA complex":169,"SCHISTOSOMA MANSONI":169,"T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell":169,"T=3 icosahedral viral capsid":169,"adenylosuccinate synthase activity":169,"alginic acid biosynthetic process":169,"carAc":169,"cobalt ion transmembrane transporter activity":169,"cobalt ion transport":169,"cytoplasmic sequestering of protein":169,"endoplasmic reticulum chaperone complex":169,"ketosteroid monooxygenase activity":169,"modulation of excitatory postsynaptic potential":169,"negative regulation of phagocytosis":169,"negative regulation of plasminogen activation":169,"nicotinamide phosphoribosyltransferase activity":169,"non-motile cilium assembly":169,"plasma membrane raft":169,"positive regulation of integrin biosynthetic process":169,"positive regulation of natural killer cell mediated cytotoxicity":169,"positive regulation of synaptic transmission, GABAergic":169,"positive regulation of transcription from RNA polymerase I promoter":169,"response to electrical stimulus":169,"retinol dehydrogenase activity":169,"sarcoplasm":169,"urate biosynthetic process":169,"(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.":168,"-!- Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds.":168,"1-chlorohexane halidohydrolase.":168,"1-haloalkane + H(2)O = a primary alcohol + halide.":168,"3-oxoacyl-[acyl-carrier-protein] synthase 2":168,"40S RIBOSOMAL PROTEIN RPS7E":168,"ATP + [protein] = diphosphate + [protein]-AMP.":168,"Adenosine monophosphate-protein transferase.":168,"Aspartate carbamoyltransferase":168,"Betaine aldehyde dehydrogenase":168,"CHLORAMPHENICOL":168,"COBALT (III) ION":168,"Carbamoylaspartic dehydrase. DHOase.":168,"DNA (147-MER)":168,"DNA-directed RNA polymerase subunit N":168,"Dihydroorotase.":168,"FRIEDLIN":168,"Haloalkane dehalogenase.":168,"INOSITOL HEXAKISPHOSPHATE":168,"Methionine gamma-lyase":168,"NS5B":168,"Pectobacterium":168,"Periplasmic [NiFe] hydrogenase large subunit":168,"SPEROIDENONE":168,"SUGAR (BETA-D-XYLOPYRANOSE)":168,"SUGAR (D-GALACTONOLACTONE)":168,"With a disulfide as acceptor.":168,"actomyosin contractile ring":168,"alkaloid biosynthetic process":168,"amine metabolic process":168,"atrioventricular canal development":168,"intrinsic apoptotic signaling pathway in response to oxidative stress":168,"mammalian, Sec61, translocation, translation, eEF2, RIBOSOME":168,"multicellular organism growth":168,"myoblast differentiation":168,"negative regulation of dopamine metabolic process":168,"negative regulation of endocytosis":168,"nuclear telomeric heterochromatin":168,"positive regulation of homocysteine metabolic process":168,"pyc, RHE_CH04002":168,"regulation of cellular protein metabolic process":168,"response to iron ion":168,"retrograde transport, endosome to Golgi":168,"transition state stabilization, substrate binding, 2-stage binding, TIM barrel (alpha/beta barrel), jelly-roll barrel, immunoglobulin, beta supersandwich, glycosidase, HYDROLASE":168,"tyrosine phosphorylation of STAT protein":168,"(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE":167,"-!- Most forms of the enzyme can rapidly hydrolyze 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyze 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. -!- This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. -!- EC 3.2.1.20 from mammalian intestine can catalyze similar reactions.":167,"3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE":167,"4-alpha-D-glucan glucohydrolase. Amyloglucosidase. Exo-1,4-alpha-glucosidase. Gamma-amylase. Glucoamylase. Lysosomal alpha-glucosidase.":167,"ATP + shikimate = ADP + shikimate 3-phosphate.":167,"B-OCTYLGLUCOSIDE":167,"Bacillus cereus ATCC 10987":167,"CELL ADHESION/IMMUNE SYSTEM":167,"Calcium-gated potassium channel mthK":167,"DECANE":167,"Giardia lamblia ATCC 50803":167,"Glucan 1,4-alpha-glucosidase.":167,"Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D- glucose.":167,"IgA binding":167,"Japanese rice":167,"Lactococcus lactis subsp. cremoris MG1363":167,"MYOSIN":167,"Phaseolus vulgaris":167,"Pyruvate decarboxylase":167,"Shikimate kinase.":167,"Streptococcus agalactiae 2603V/R":167,"Streptomyces avermitilis":167,"Streptomyces sp.":167,"Streptomyces venezuelae":167,"bread wheat":167,"catecholamine biosynthetic process":167,"ciliary membrane":167,"glycosaminoglycan binding":167,"histone mRNA metabolic process":167,"medicinal leech":167,"microtubule plus-end binding":167,"mitochondrial alpha-ketoglutarate dehydrogenase complex":167,"myosin II complex":167,"neuron remodeling":167,"phagolysosome":167,"positive regulation of alpha-beta T cell differentiation":167,"positive regulation of macrophage derived foam cell differentiation":167,"positive regulation of natural killer cell chemotaxis":167,"regulation of embryonic development":167,"regulation of smoothened signaling pathway":167,"response to abscisic acid":167,"structural molecule activity conferring elasticity":167,"tau protein binding":167,"-!- Involved in the biosynthesis of lysine in bacteria, cyanobacteria and higher plants. -!- Earlier erroneously called 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase.":166,"2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase":166,"2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase.":166,"78-meric":166,"Acyl-CoA dehydrogenase":166,"Aspergillus flavus":166,"BACTERIOFERRITIN":166,"Chaperone":166,"DNA-directed RNA polymerase subunit K":166,"ErbB-3 class receptor binding":166,"Glucokinase":166,"Lysine-specific histone demethylase 1A":166,"Mannose-Binding Protein A, subunit A":166,"Nuclear receptor-interacting peptide":166,"PROTEIN (LYSOZYME)":166,"Parabacteroides distasonis":166,"Ribosomal protein RACK1":166,"Ribosomal protein eS1":166,"Ribosomal protein eS10":166,"Ribosomal protein eS12":166,"Ribosomal protein eS17":166,"Ribosomal protein eS19":166,"Ribosomal protein eS21":166,"Ribosomal protein eS24":166,"Ribosomal protein eS26":166,"Ribosomal protein eS27":166,"Ribosomal protein eS28":166,"Ribosomal protein eS30":166,"Ribosomal protein eS31":166,"Ribosomal protein eS4":166,"Ribosomal protein eS6":166,"Ribosomal protein eS7":166,"Ribosomal protein eS8":166,"Ribosomal protein uS10":166,"Ribosomal protein uS13":166,"Ribosomal protein uS14":166,"Ribosomal protein uS15":166,"Ribosomal protein uS17":166,"Ribosomal protein uS19":166,"Ribosomal protein uS2":166,"Ribosomal protein uS3":166,"Ribosomal protein uS4":166,"Ribosomal protein uS5":166,"Ribosomal protein uS7":166,"Ribosomal protein uS8":166,"Ribosomal protein uS9":166,"Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate.":166,"Succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. Tetrahydrodipicolinate N-succinyltransferase. Tetrahydrodipicolinate succinylase. Tetrahydrodipicolinate succinyltransferase.":166,"apoptotic cell clearance":166,"carboxypeptidase activity":166,"chloride channel regulator activity":166,"electron transport chain":166,"negative regulation of histone H3-K9 methylation":166,"neuromuscular process controlling balance":166,"phosphatidylcholine binding":166,"transcription of nuclear large rRNA transcript from RNA polymerase I promoter":166,"-!- Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D- ribose 5-phosphate. -!- Alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5- bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.6.":165,"14579":165,"Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.":165,"Cholera enterotoxin subunit B":165,"DNA polymerase III subunit delta":165,"DNA supercoiling activity":165,"Deoxyribomutase. Deoxyribose phosphomutase. Phosphodeoxyribomutase.":165,"Desulfitobacterium hafniense":165,"Echinophyllia sp. SC22":165,"GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297, S4564":165,"HIST1H2AB, H2AFM, HIST1H2AE, H2AFA":165,"HIST1H2BJ, H2BFR":165,"Haloalkane dehalogenase":165,"M145":165,"Phosphopentomutase.":165,"Rossmann Fold, Oxidoreductase, Dihydroorotate/orotate and fumarate/succinate binding, Cytosol, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex":165,"SUGAR (B-NONYLGLUCOSIDE)":165,"Stenotrophomonas maltophilia":165,"THREONINE":165,"Trichomonas vaginalis":165,"[acyl-carrier-protein] S-malonyltransferase activity":165,"bile acid signaling pathway":165,"ceramide biosynthetic process":165,"glucosylceramidase activity":165,"limb development":165,"negative regulation of complement activation":165,"positive regulation of glucose metabolic process":165,"positive regulation of mRNA catabolic process":165,"positive regulation of potassium ion transport":165,"positive regulation of synapse assembly":165,"-!- The HslU subunit of the HslU--HslV complex functions as an ATP dependent 'unfoldase'. -!- The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. -!- HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. -!- Belongs to peptidase family T1.":164,"27634":164,"ARG1":164,"ATP + sulfate = diphosphate + adenylyl sulfate.":164,"ATP-dependent cleavage of peptide bonds with broad specificity.":164,"ATP-dependent zinc metalloprotease FtsH":164,"ATP-sulfurylase. Sulfate adenylate transferase. Sulfurylase.":164,"Actinomadura sp. R39":164,"Alpha-L-fucosidase":164,"CD8 receptor binding":164,"Cell division control protein 21":164,"DNA POLYMERASE I":164,"DNA-N1-methyladenine dioxygenase activity":164,"DNA-directed RNA polymerase subunit P":164,"DODECANE":164,"Death-associated protein kinase 1":164,"EGFR, ERBB1":164,"HslU--HslV peptidase.":164,"Human immunodeficiency virus type 1 group M subtype B (isolate BH10)":164,"M1 family aminopeptidase":164,"PcG protein complex":164,"Polymerase acidic protein":164,"Portal protein":164,"RNA polymerase sigma factor":164,"SNARE complex assembly":164,"SUGAR-BINDING PROTEIN":164,"Sucrose isomerase":164,"Sulfate adenylyltransferase.":164,"Tyrosine-protein kinase Lck":164,"beta-alanine metabolic process":164,"cellular response to jasmonic acid stimulus":164,"demethylase activity":164,"dihydrofolate metabolic process":164,"folate reductase activity":164,"myosin filament":164,"neurotransmitter biosynthetic process":164,"protein phosphatase inhibitor activity":164,"regulation of B cell apoptotic process":164,"ribosomal large subunit assembly":164,"(E3-independent) E2 ubiquitin-conjugating enzyme.":163,"-!- The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). -!- It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg(2+)-ATP and catalyzes the conjugation of ubiquitin to protein substrates, independently of E3. -!- This transfer has only been observed with small proteins. -!- In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L- lysine methyl ester) has been observed.":163,"2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE":163,"3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ":163,"ALK tyrosine kinase receptor":163,"CELLULAR TUMOR ANTIGEN P53":163,"Chlamydia trachomatis":163,"Cytochrome P450":163,"DANIO RERIO":163,"DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE":163,"E3-independent ubiquitin-conjugating enzyme E2.":163,"Elongin-C":163,"Helix hairpin bin":163,"Holo-[acyl-carrier-protein] synthase":163,"Hypoxanthine-guanine phosphoribosyltransferase":163,"ITGA2B, GP2B, ITGAB":163,"Non-structural protein 1":163,"Pectobacterium atrosepticum":163,"S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N(6)- monoubiquitinyl-[acceptor protein]-L-lysine.":163,"Thermococcus kodakaraensis":163,"antibody-dependent cellular cytotoxicity":163,"bone resorption":163,"cysteine biosynthetic process":163,"heme oxygenase (decyclizing) activity":163,"magnesium ion transmembrane transport":163,"negative regulation of G-protein coupled receptor protein signaling pathway":163,"positive regulation of activation of Janus kinase activity":163,"positive regulation of chondrocyte proliferation":163,"protein phosphatase regulator activity":163,"pyrimidine dimer repair":163,"response to fluid shear stress":163,"skeletal muscle cell differentiation":163,"specific granule":163,"termination of signal transduction":163,"-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7.":162,"2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC ACID":162,"2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase.":162,"3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE":162,"49558":162,"BETA-LACTAMASE":162,"Bacillus pumilus":162,"Bartonella henselae":162,"CCNA2, CCN1, CCNA":162,"Cryptosporidium":162,"Cupredoxins -  blue copper proteins":162,"DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide":162,"Desulfovibrio fructosivorans":162,"ELECTRON TRANSFER":162,"Flavivirus":162,"MHC class I receptor activity":162,"Mitogen-activated protein kinase 10":162,"Pentameric":162,"Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+).":162,"Pyruvate synthase.":162,"RECOMBINATION/DNA":162,"RNA (1504-MER)":162,"Response regulator":162,"SUGAR (CELLOBIOSE)":162,"Sialidase B":162,"Superoxide dismutase [Fe]":162,"UNP residues 25-299":162,"VIRUS, GFLV, FANLEAF DISEASE":162,"chitinase activity":162,"eye development":162,"homocysteine metabolic process":162,"imaginal disc-derived wing morphogenesis":162,"ligand-binding domain":162,"mauA":162,"methionine adenosyltransferase activity":162,"multicellular organismal response to stress":162,"neutrophil migration":162,"tRNA processing":162,"transcription initiation from RNA polymerase I promoter":162,"ventricular cardiac muscle tissue morphogenesis":162,"(3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE":161,"-!- Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). -!- These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which lead to the apoptotic phenotype. -!- Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect. -!- Caspase-7 is activated by the initiator caspases (caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)). -!- Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits. -!- Belongs to peptidase family C14.":161,"1-deoxy-D-xylulose-5-phosphate reductoisomerase activity":161,"6-HYDROXYURIDINE-5'-PHOSPHATE":161,"9 REPEAT DOMAINS, PROTEIN-PROTEIN COMPLEX, Ribonucleoprotein, STRUCTURAL PROTEIN":161,"93TH057":161,"Aminoacyl-tRNA hydrolase.":161,"Apoptotic protease Mch-3. CASP-7. CMH-1. ICE-LAP3. ICE-like apoptotic protease 3. Mch3.":161,"CYTOCHROME C":161,"Caspase-7":161,"Caspase-7.":161,"D-ALANINE":161,"DNA-directed RNA polymerase omega chain":161,"Elongin-B":161,"HRAS, HRAS1":161,"Hepatitis C virus subtype 1a":161,"Hirudo":161,"N-substituted aminoacyl-tRNA + H(2)O = N-substituted amino acid + tRNA.":161,"NADPH oxidation":161,"NQO2, NMOR2":161,"PA-I galactophilic lectin":161,"Peptidyl-tRNA hydrolase.":161,"Plasmodium falciparum Vietnam Oak-Knoll (FVO)":161,"Pseudomonas phage phi12":161,"Reverse transcriptase":161,"SIGNALING PROTEIN/INHIBITOR":161,"Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.":161,"TATA-box-binding protein":161,"Vinculin":161,"adult locomotory behavior":161,"anterior/posterior pattern specification":161,"carnitine metabolic process":161,"cobalamin binding":161,"cyclin/CDK positive transcription elongation factor complex":161,"galactose metabolic process":161,"genitalia development":161,"host cell Golgi apparatus":161,"integral component of cell outer membrane":161,"negative regulation of toll-like receptor 9 signaling pathway":161,"peptidoglycan binding":161,"positive regulation of proteolysis involved in cellular protein catabolic process":161,"regulation of cellular senescence":161,"ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor":161,"sigma factor activity":161,"viral protein":161,"-!- An endoribonuclease that cleaves double-stranded RNA molecules. -!- The cleavage can be either a single-stranded nick or double-stranded break in the RNA, depending in part upon the degree of base-pairing in the region of the cleavage site. -!- Specificity is conferred by negative determinants, i.e., the presence of certain Watson-Crick base-pairs at specific positions that strongly inhibit cleavage. -!- RNase III is involved in both rRNA processing and mRNA processing and decay.":160,"-!- Comprises bacterial enzymes that import maltose and maltose oligosaccharides.":160,"-!- Does not act on nucleoside monophosphates. -!- Induced in Escherichia coli by T-even phages.":160,"10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide.":160,"10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.":160,"10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4- imidazolecarboxamide formyltransferase. 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase. 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase. 5-amino-4-imidazolecarboxamide ribonucleotide transformylase. 5-amino-4-imidazolecarboxamide ribotide transformylase. AICAR formyltransferase. AICAR transformylase. Aminoimidazolecarboxamide ribonucleotide transformylase.":160,"2-amino-N-ribosylacetamide 5'-phosphate transformylase. 5'-phosphoribosylglycinamide transformylase. 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase. GAR formyltransferase. GAR TFase. GAR transformylase. GART. Glycinamide ribonucleotide transformylase.":160,"40S ribosomal protein S3":160,"5'-polynucleotidase. Polynucleotide 5'-triphosphatase.":160,"A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.":160,"ATP + H(2)O + maltose(Out) = ADP + phosphate + maltose(In).":160,"ATP phosphoribosyltransferase":160,"Acinetobacter baumannii AYE":160,"Antithrombin-III":160,"BAA-125":160,"BRCA1-A complex":160,"Bacteriophage T4":160,"DIPHOSPHATE":160,"DNA polymerase III subunit delta'":160,"Equus":160,"FLUORIDE ION":160,"Finegoldia magna":160,"Golgi alpha-mannosidase II":160,"Gram-negative-bacterium-type cell outer membrane assembly":160,"Growth factor receptor-bound protein 2":160,"H2-K1, H2-K":160,"HEXATANTALUM DODECABROMIDE":160,"HYDROLASE/HYDROLASE inhibitor":160,"Interleukin-1 receptor-associated kinase 4":160,"L-LACTATE DEHYDROGENASE":160,"LYASE/METAL BINDING PROTEIN":160,"MT3707, MTCY07H7B.20, panC, Rv3602c":160,"Maltose-transporting ATPase.":160,"Mitochondrial cytochrome c1, heme protein":160,"NITRITE REDUCTASE":160,"Nuclear receptor, transcription factor, ligand binding, protein-ligand complex, TRANSCRIPTION":160,"OXYGEN BINDING":160,"Phosphoribosylaminoimidazolecarboxamide formyltransferase.":160,"Phosphoribosylglycinamide formyltransferase.":160,"Polynucleotide 5'-phosphatase.":160,"Ribonuclease 3. RNase III.":160,"Ribonuclease III.":160,"Thermobifida fusca YX":160,"Toxoplasma":160,"VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR":160,"cysteine biosynthetic process from serine":160,"hemostasis":160,"necroptotic signaling pathway":160,"negative regulation of mRNA polyadenylation":160,"neutrophil activation":160,"nucleocytoplasmic transport":160,"nucleoside triphosphate biosynthetic process":160,"phenanthrene 9,10-monooxygenase activity":160,"positive regulation of calcium-mediated signaling":160,"positive regulation of fatty acid biosynthetic process":160,"positive regulation of keratinocyte apoptotic process":160,"positive regulation of toll-like receptor 4 signaling pathway":160,"protein adenylyltransferase activity":160,"reciprocal meiotic recombination":160,"regulation of establishment of T cell polarity":160,"regulation of plasma membrane raft polarization":160,"regulation of protein heterodimerization activity":160,"regulation of receptor clustering":160,"regulation of wound healing, spreading of epidermal cells":160,"renal protein absorption":160,"response to auxin":160,"small GTPase binding":160,"striated muscle atrophy":160,"(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID":159,"-!- The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23.":159,"10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH.":159,"10-formyltetrahydrofolate dehydrogenase.":159,"3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC":159,"5.8S RRNA":159,"ABO":159,"Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate.":159,"Beta-lactamase TEM":159,"Bifunctional protein GlmU":159,"CELLVIBRIO JAPONICUS":159,"D-galactonate dehydratase family member ManD":159,"DNA methylation":159,"Formyltetrahydrofolate dehydrogenase.":159,"Glucosamine-1-phosphate N-acetyltransferase.":159,"Murine norovirus 1":159,"Pectobacterium atrosepticum SCRI1043":159,"Pyruvate synthase":159,"RESIDUES 2-132":159,"SUGAR (2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL)":159,"Toxin":159,"Urease subunit beta":159,"activin receptor signaling pathway":159,"cytochrome c1":159,"hormone binding":159,"inner ear morphogenesis":159,"negative regulation of Wnt signaling pathway":159,"negative regulation of adenylate cyclase activity":159,"ovarian follicle development":159,"p51":159,"p66":159,"phosphorelay sensor kinase activity":159,"positive regulation of calcidiol 1-monooxygenase activity":159,"positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway":159,"pyrimidine nucleotide metabolic process":159,"regulation of protein homodimerization activity":159,"regulation of short-term neuronal synaptic plasticity":159,"response to cocaine":159,"sarcomere":159,"5'-3' exonuclease activity":158,"ASPERGILLUS FUMIGATUS":158,"Amicyanin":158,"Azotobacter":158,"Burkholderia xenovorans":158,"CYTOSOL":158,"Ephrin type-A receptor 2":158,"Escherichia phage N4":158,"Ferritin heavy chain":158,"Multidrug resistance protein MexB":158,"Neopullulanase 2":158,"Nitric-oxide synthase, brain":158,"PHOTOSYNTHETIC REACTION CENTER":158,"Phosphopentomutase":158,"Polymerase cofactor VP35":158,"RESIDUES 54-213":158,"SUGAR (FRUCTOSE-2,6-DIPHOSPHATE)":158,"Spike glycoprotein":158,"Thermoplasma volcanium GSS1":158,"Virion DNA-directed RNA polymerase":158,"age-dependent response to reactive oxygen species":158,"cell activation":158,"cellular response to phosphate starvation":158,"negative regulation of integrin biosynthetic process":158,"negative regulation of keratinocyte proliferation":158,"polA, GK2730":158,"positive regulation of transforming growth factor beta receptor signaling pathway":158,"protein phosphatase type 2A complex":158,"regulation of IRE1-mediated unfolded protein response":158,"regulation of microtubule cytoskeleton organization":158,"ubiquitin-ubiquitin ligase activity":158,"uridine phosphorylase activity":158,"viral protein/immune system":158,"-!- Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)- acetylspermidine and N(8)-acetylspermidine.":157,"-!- The enzyme participates in the pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). -!- The enzyme exists in varying types of multifunctional proteins in different organisms. -!- The enzyme from the bacterium Streptococcus pneumoniae also harbors the activity of EC 4.1.2.25, the enzyme from the plant Arabidopsis thaliana harbors the activity of EC 2.5.1.15, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities.":157,"2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.":157,"2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. 6-hydroxymethyl-7,8-dihydropterin diphosphokinase. 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase. 7,8-dihydro-6-hydroxymethylpterin diphosphokinase. 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase.":157,"ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8- dihydropterin diphosphate.":157,"ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.":157,"Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.":157,"Acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase. Diamine acetyltransferase. Putrescine (diamine)-acetylating enzyme. Putrescine acetylase. Putrescine acetyltransferase. Putrescine N-acetyltransferase. Spermidine acetyltransferase. Spermidine N(1)-acetyltransferase.":157,"Acetylglutamate kinase.":157,"Arginase":157,"BRCA1-BARD1 complex":157,"C-terminal fragment":157,"Caulobacter crescentus":157,"Diamine N-acetyltransferase.":157,"Dual specificity tyrosine-phosphorylation-regulated kinase 1A":157,"EPHX2":157,"Ferredoxin-1":157,"Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1":157,"HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512":157,"House Mouse":157,"K63-linked polyubiquitin binding":157,"METHYLTRANSFERASE":157,"Major capsid protein VP1":157,"Methyl-accepting chemotaxis protein":157,"Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2":157,"NUCLEOSIDE DIPHOSPHATE KINASE":157,"Ptgs2, Cox-2, Cox2, Pghs-b, Tis10":157,"basement membrane disassembly":157,"hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides":157,"intermediate-density lipoprotein particle":157,"nuclear export":157,"phosphatidic acid binding":157,"protein targeting to vacuole":157,"ribosome structure, protein-RNA complex, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, Antibiotic resistance, Repressor, Transcription, Transcription regulation, Transcription termination, Translation regulation, tRNA-binding, Methylation, Endonuclease, Hydrolase, Nuclease, RIBOSOME":157,"-!- Also acts slowly with CTP. -!- Catalyzes template-independent extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- The primer, depending on the source of the enzyme, may be an RNA or DNA fragment or oligo(A) bearing a 3'-OH terminal group. -!- See also EC 2.7.7.6.":156,"-!- The enzyme cleaves a carbon-sulfur bond, releasing methanethiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- The enzyme is involved in L-methionine catabolism.":156,"-!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.":156,"78 kDa glucose-regulated protein":156,"ATCC BAA-679 / EGD-e":156,"ATP + RNA(n) = diphosphate + RNA(n+1).":156,"ATPase activator activity":156,"Blue copper oxidase CueO":156,"CATALYTIC DOMAIN (RESIDUES 441-875)":156,"Collagenase 3":156,"Cysteine desulfurase.":156,"Cysteine desulfurylase.":156,"DDX58":156,"Flemming body":156,"Glutamyl-tRNA(Gln) amidotransferase subunit A":156,"Heme oxygenase 1":156,"Insulin-like growth factor 1 receptor":156,"Interleukin-2":156,"Isocitrate dehydrogenase [NADP]":156,"L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.":156,"L-methioninase. Methionine lyase.":156,"L-methionine + H(2)O = methanethiol + NH(3) + 2-oxobutanoate.":156,"Lethal factor":156,"Methionine gamma-lyase.":156,"Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i":156,"NTP polymerase. Poly(A) polymerase. RNA adenylating enzyme.":156,"NTPase P4":156,"PCSK9-LDLR complex":156,"Phosphocarrier protein HPr":156,"Polynucleotide adenylyltransferase.":156,"SUGAR (O1-METHYL-MANNOSE)":156,"TETRADECANOYL-COA":156,"THROMBIN":156,"TRANSCRIPTION, TRANSFERASE/DNA-RNA HYBRID":156,"U6 snRNP":156,"ZEBOV":156,"Zymomonas":156,"adenine/cytosine mispair binding":156,"amidase activity":156,"bacterial-type RNA polymerase core promoter sequence-specific DNA binding":156,"box C/D snoRNP assembly":156,"cellular response to fatty acid":156,"chromosome passenger complex":156,"decoding, Streptomycin, RNA structure, antibiotic resistance, RIBOSOME":156,"endosome organization":156,"inactivation of MAPKK activity":156,"kynurenine-oxoglutarate transaminase activity":156,"llama":156,"lymph node development":156,"mammary gland involution":156,"negative regulation of long-term synaptic potentiation":156,"negative regulation of toll-like receptor 2 signaling pathway":156,"positive regulation of NFAT protein import into nucleus":156,"positive regulation of cell migration involved in sprouting angiogenesis":156,"regulation of G-protein coupled receptor protein signaling pathway":156,"threonine-tRNA ligase activity":156,"-!- A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. -!- This enzyme transports Cu(+) or Ag(+), and cannot transport the divalent ions, contrary to EC 3.6.3.4, which mainly transports the divalent copper ion. -!- Formerly EC 3.6.3.n1.":155,"-!- Also acts on glucosylsphingosine (cf. EC 3.2.1.62).":155,"-!- Converts amylose into amylopectin. -!- The description (official name) requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. -!- The latter has frequently been termed Q-enzyme.":155,"-!- The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). -!- The enzyme exists in varying types of multifunctional proteins in different organisms. -!- The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25.":155,"1,4-alpha-glucan branching enzyme.":155,"6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.":155,"ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2).":155,"Acid beta-glucosidase. Beta-glucocerebrosidase. D-glucosyl-N-acylsphingosine glucohydrolase.":155,"Amylo-(1,4 to 1,6)transglucosidase. Amylo-(1,4->1,6)-transglycosylase. Branching enzyme. Glycogen branching enzyme.":155,"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B":155,"CASP3, CPP32":155,"CATALYTIC DOMAIN, RESIDUES 50-212":155,"COMPLEMENT C3B ALPHA' CHAIN":155,"COPII vesicle coat":155,"Cu(+) exporting ATPase.":155,"Cytochrome b-c1 complex subunit 6":155,"D-glucosyl-N-acylsphingosine + H(2)O = D-glucose + N-acylsphingosine.":155,"DHPS. Dihydropteroate diphosphorylase. Dihydropteroate pyrophosphorylase.":155,"Dihydropteroate synthase.":155,"Enterobacter":155,"Escherichia coli O139:H28 str. E24377A":155,"Ferredoxin CarAc":155,"Glucosylceramidase":155,"Glucosylceramidase.":155,"HHV-1":155,"MERCURIBENZOIC ACID":155,"Pyrobaculum ferrireducens":155,"Rhodospirillum":155,"SYNECHOCOCCUS ELONGATUS":155,"Serratia":155,"TRANSFERASE/PEPTIDE":155,"Transferred entry: 1.8.99.5.":155,"Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.":155,"arginine metabolic process":155,"cell fate commitment":155,"clathrin coat assembly":155,"coumarin metabolic process":155,"glucosylceramide catabolic process":155,"kynurenine metabolic process":155,"lysine N-acetyltransferase activity, acting on acetyl phosphate as donor":155,"negative regulation of Notch signaling pathway":155,"negative regulation of defense response to virus by host":155,"negative regulation of endoribonuclease activity":155,"negative regulation of gene silencing by miRNA":155,"positive regulation of immunoglobulin secretion":155,"positive regulation of neuronal action potential":155,"positive regulation of protein lipidation":155,"regulation of lysosomal protein catabolic process":155,"retinal ganglion cell axon guidance":155,"selenocysteine metabolic process":155,"transcription corepressor binding":155,"trophectodermal cell differentiation":155,"ubiquinone biosynthetic process":155,"(MOLYBDOPTERIN-CYTOSINE DINUCLEOTIDE-S,S)-DIOXO-AQUA-MOLYBDENUM(V)":154,"-!- Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). -!- Formerly EC 5.3.1.19.":154,"-!- Viruses that are members of the Norovirus genus (Caliciviridae family) are a major cause of epidemic acute viral gastroenteritis. -!- The nonstructural proteins of these viruses are produced by proteolytic cleavage of a large precursor polyprotein, performed by a protease that is incorporated into the polyprotein. -!- Cleavage sites are apparently defined by features based on both sequence and structure since several sites in the polyprotein fulfilling the identified sequence requirements are not cleaved. -!- The presence of acidic (Asp), basic (Arg), aromatic (Tyr) or aliphatic (Leu) amino acids at the P1' position results in only minor differences in cleavage efficiency, suggesting that steric or conformational constraints may play a role in determining specificity. -!- Changes to the amino acid at the P2 position do not alter cleavage efficiency. -!- Belongs to peptidase family C37.":154,"1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE":154,"15-CIS-1,2-DIHYDRONEUROSPORENE":154,"3-isopropylmalate dehydrogenase":154,"4'-PHOSPHOPANTETHEINE":154,"Acetobacter":154,"BACTERIOPHAGE PHI12":154,"CCR1 chemokine receptor binding":154,"Calicivirin.":154,"Calicivirus 3C-like protease. Calicivirus endopeptidase. Calicivirus TCP. Calicivirus trypsin-like cysteine protease. Camberwell virus processing peptidase. Chiba virus processing peptidase. Norovirus virus processing peptidase. Norwalk virus processing peptidase. Rabbit hemorrhagic disease virus 3C endopeptidase. Southampton virus processing peptidase.":154,"D-fructose-6-phosphate amidotransferase. GlcN6P synthase. Glucosamine-6-phosphate isomerase (glutamine-forming). Glucosamine-6-phosphate synthase. Hexosephosphate aminotransferase. L-glutamine-D-fructose-6-phosphate amidotransferase.":154,"DNA MISMATCH REPAIR PROTEIN MUTS":154,"Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.":154,"GADOLINIUM ATOM":154,"Glutamine--fructose-6-phosphate transaminase (isomerizing).":154,"Herpes simplex virus (type 1 / strain 17)":154,"L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.":154,"Methanosarcina":154,"Multidrug resistance protein MexA":154,"N":154,"NAD-dependent histone deacetylase activity":154,"NTPASE P4":154,"Na, K-ATPase alpha subunit":154,"PHOSPHORIC ACID MONO(FORMAMIDE)ESTER":154,"Phospholemman-like protein":154,"Sulfolobus shibatae":154,"T cell homeostasis":154,"autophagosome assembly":154,"cholinesterase activity":154,"cysteine metabolic process":154,"embryonic morphogenesis":154,"hist1h2aj, LOC494591":154,"induction by virus of host cell-cell fusion":154,"interleukin-16 binding":154,"interleukin-16 receptor activity":154,"leucine biosynthetic process":154,"maintenance of protein localization in endoplasmic reticulum":154,"neuron projection morphogenesis":154,"neurotrophin binding":154,"odontogenesis of dentin-containing tooth":154,"protein-arginine omega-N asymmetric methyltransferase activity":154,"regulation of ATF6-mediated unfolded protein response":154,"regulation of PERK-mediated unfolded protein response":154,"regulation of amyloid precursor protein catabolic process":154,"regulation of axon regeneration":154,"regulation of endoplasmic reticulum unfolded protein response":154,"regulation of gene expression, epigenetic":154,"regulation of protein folding in endoplasmic reticulum":154,"regulation of reactive oxygen species metabolic process":154,"response to organophosphorus":154,"sperm individualization":154,"transcription antitermination":154,"viral genome maturation":154,"-!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399.":153,"-!- The enzyme acts on multiple 3-alpha-hydroxysteroids, such as androsterone and 5 alpha-dihydrotestosterone. -!- The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation. -!- This entry stands for enzymes whose stereo-specificity with respect to NAD(+) or NADP(+) is not known (cf. EC 1.1.1.50 and EC 1.1.1.213).":153,"3'-5'-exodeoxyribonuclease activity":153,"3-alpha-hydroxysteroid 3-dehydrogenase.":153,"3-alpha-hydroxysteroid dehydrogenase.":153,"3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH.":153,"3-phosphoglycerate dehydrogenase. 3-phosphoglyceric acid dehydrogenase. 3PHP reductase. Alpha-KG reductase. Alpha-phosphoglycerate dehydrogenase. D-3-phosphoglycerate dehydrogenase. Glycerate 3-phosphate dehydrogenase. Glycerate-1,3-phosphate dehydrogenase. PGDH. Phosphoglycerate oxidoreductase. Phosphoglyceric acid dehydrogenase.":153,"33970":153,"A/P-site tRNA":153,"AIR synthase. AIR synthetase. AIRS. Phosphoribosyl-aminoimidazole synthetase. Phosphoribosylaminoimidazole synthetase.":153,"ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1":153,"ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.":153,"Alkyl hydroperoxide reductase subunit C":153,"Brevundimonas diminuta":153,"Carbon monoxide dehydrogenase large chain":153,"Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha":153,"Catalytic Domain":153,"DNA (5'-D(*CP*TP*AP*CP*CP*GP*AP*TP*AP*AP*GP*CP*AP*GP*AP*CP*GP*AP*TP*CP*CP*TP*CP*TP*CP*GP*AP*TP*G)-3')":153,"DNA-DIRECTED RNA POLYMERASE":153,"GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE":153,"GSK3B":153,"HYDROXY(DIOXO)MOLYBDENUM":153,"Halorhodospira halophila":153,"IGKC":153,"Induced myeloid leukemia cell differentiation protein Mcl-1":153,"Integrin beta-2":153,"MALEIC ACID":153,"METAL-BINDING PROTEIN":153,"Mastigocladus laminosus":153,"Methyl-coenzyme M reductase I subunit alpha":153,"Phosphoglycerate dehydrogenase.":153,"Phosphoribosylformylglycinamidine cyclo-ligase.":153,"Putative hydrolase":153,"TRNA-LEU":153,"TRNA-TYR":153,"Toll-like receptor 2 binding":153,"Transcription termination factor Rho":153,"UNP residues 237-773":153,"creatine kinase activity":153,"dorsal/ventral pattern formation":153,"hemolysis in other organism":153,"hybridoma":153,"modulation by virus of host transcription":153,"nitrogen catabolite activation of transcription from RNA polymerase II promoter":153,"oxidoreductase activity, oxidizing metal ions":153,"peptidoglycan metabolic process":153,"protein transmembrane transporter activity":153,"retinal metabolic process":153,"suppression by virus of host MAVS activity by MAVS proteolysis":153,"transcription factor activity, TFIID-class binding":153,"(S)-2-haloacid + H(2)O = (R)-2-hydroxyacid + halide.":152,"(S)-2-haloacid dehalogenase.":152,"-!- ADP, IDP, GDP, UDP and CDP can act as donors.":152,"-!- Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 (see also EC 3.8.1.9, EC 3.8.1.10 and EC 3.8.1.11).":152,"-!- Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion.":152,"-!- Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A. -!- An enzyme from Pseudomonas aeruginosa also acts on butirosin.":152,"1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D- ribose 1-diphosphate.":152,"104":152,"2-haloacid dehalogenase. 2-haloacid halidohydrolase. 2-haloalkanoic acid dehalogenase. 2-haloalkanoid acid halidohydrolase. 2-halocarboxylic acid dehalogenase II. DL-2-haloacid dehalogenase. Halocarboxylic acid halidohydrolase. L-2-haloacid dehalogenase. L-DEX.":152,"4-alpha-D-glucan maltohydrolase. Glycogenase. Saccharogen amylase.":152,"40S ribosomal protein S2":152,"5'-flap endonuclease activity":152,"ASPARAGINE":152,"ATP + kanamycin = ADP + kanamycin 3'-phosphate.":152,"ATP phosphoribosyltransferase.":152,"ATP synthase gamma chain":152,"Aminoglycoside 3'-phosphotransferase. APH(3'). Neomycin-kanamycin phosphotransferase.":152,"Arcobacter butzleri RM4018":152,"Aspartokinase":152,"BINDING PROTEIN":152,"Beta-amylase.":152,"Cupriavidus metallidurans CH34":152,"Escherichia virus MS2":152,"Ferredoxin":152,"Fucose-binding lectin PA-IIL":152,"Geobacter metallireducens GS-15":152,"Glutamate racemase.":152,"Golgi reassembly":152,"HIV-1 protease":152,"Histone-arginine methyltransferase CARM1":152,"Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.":152,"INFLUENZA A VIRUS":152,"Kanamycin kinase.":152,"L-glutamate = D-glutamate.":152,"Phosphoribosyl-ATP diphosphorylase. Phosphoribosyl-ATP pyrophosphorylase.":152,"Polynucleotide phosphorylase.":152,"Polyribonucleotide nucleotidyltransferase.":152,"Pseudomonas mendocina":152,"RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.":152,"Roundabout signaling pathway":152,"Vanillyl-alcohol oxidase":152,"chemokine receptor binding":152,"clpP":152,"depurination":152,"exon-exon junction complex":152,"hypothetical protein yedk domain like":152,"hypoxanthine phosphoribosyltransferase activity":152,"negative regulation of stem cell differentiation":152,"nuclear-transcribed mRNA catabolic process, exonucleolytic":152,"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor":152,"p38MAPK cascade":152,"positive regulation of G1/S transition of mitotic cell cycle":152,"positive regulation of epidermal growth factor-activated receptor activity":152,"positive regulation of filopodium assembly":152,"positive regulation of interleukin-8 secretion":152,"positive regulation of isotype switching":152,"positive regulation of mast cell chemotaxis":152,"protein repair":152,"proton-transporting ATP synthase complex, catalytic core F(1)":152,"single strand break repair":152,"very-low-density lipoprotein particle receptor binding":152,"-!- Cutin, a polymeric structural component of plant cuticles, is an hydroxy fatty acid polymer, usually C(16) or C(18) and that contains one to three hydroxyl groups. -!- The enzyme from several fungal sources also hydrolyzes the p-nitrophenyl esters of hexadecanoic acid. -!- It is however inactive toward several esters that are substrates for non-specific esterases.":151,"-!- This microsomal enzyme catalyzes the first committed step in the biosynthesis of sterols. -!- In the absence of NAD(P)H, presqualene diphosphate (PSPP) is accumulated. -!- When NAD(P)H is present, presqualene diphosphate does not dissociate from the enzyme during the synthesis of squalene from farnesyl diphosphate (FPP). -!- High concentrations of FPP inhibit the production of squalene but not of PSPP.":151,"-!- While nitroethane may be the physiological substrate, the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols. -!- Differs from EC 1.13.12.16 in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates.":151,"1-pyrroline-5-carboxylate dehydrogenase activity":151,"2 farnesyl diphosphate + NAD(P)H = squalene + 2 diphosphate + NAD(P)(+).":151,"50S RIBOSOMAL PROTEIN L7AE":151,"A nitroalkane + H(2)O + O(2) = an aldehyde or ketone + nitrite + H(2)O(2).":151,"ANTIGEN-BINDING FRAGMENT, FAB":151,"CATALASE":151,"Cutin + H(2)O = cutin monomers.":151,"Cutin hydrolase.":151,"Cutinase.":151,"Cytochrome c oxidase subunit 4 isoform 1, mitochondrial":151,"Cytochrome c oxidase subunit 5A, mitochondrial":151,"Cytochrome c oxidase subunit 5B, mitochondrial":151,"Cytochrome c oxidase subunit 6A2, mitochondrial":151,"Cytochrome c oxidase subunit 7A1, mitochondrial":151,"Cytochrome c oxidase subunit 7B, mitochondrial":151,"Cytochrome c oxidase subunit 7C, mitochondrial":151,"Cytochrome c oxidase subunit 8B, mitochondrial":151,"Cytochrome c1":151,"EMERICELLA NIDULANS":151,"Ebola virus - Mayinga, Zaire, 1976":151,"Farnesyl-diphosphate farnesyltransferase. Farnesyltransferase. Presqualene synthase. Presqualene-diphosphate synthase. Squalene synthetase.":151,"Influenza A virus (A/Brevig Mission/1/1918(H1N1))":151,"Malate synthase G":151,"NA":151,"NAO. Nitroethane oxidase. Nitroethane reductase.":151,"NICOTINAMIDE":151,"Nitroalkane oxidase.":151,"O-methyltransferase activity":151,"Squalene synthase.":151,"Staphylococcus epidermidis RP62A":151,"Synechococcus sp. PCC 7002":151,"Tyrosine-protein phosphatase non-receptor type 11":151,"WD repeat-containing protein 5":151,"aggresome assembly":151,"cholesterol binding":151,"chronic inflammatory response to antigenic stimulus":151,"ferredoxin-NADP+ reductase activity":151,"ferrochelatase activity":151,"groL, groEL, mopA, b4143, JW4103":151,"hydroquinone:oxygen oxidoreductase activity":151,"late endosome to vacuole transport":151,"m7G(5')pppN diphosphatase activity":151,"mannan binding":151,"nucleoside diphosphate phosphorylation":151,"protein channel activity":151,"regulation of translational termination":151,"(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate.":150,"(4S)-4-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3lambda~5~-thiazol-2-yl}-4-hydroxybutanoic acid":150,"-!- Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols. -!- The enol form (2Z,4E)-2-hydroxyhexa-2,4-dienedioate is produced as part of this pathway and is converted to the keto form (3E)-2-oxohex- 3-enedioate by the enzyme. -!- Another keto form, (4E)-2-oxohex-4-enedioate (4-oxalocrotonate), was originally thought to be produced by the enzyme but later shown to be produced non-enzymatically.":150,"-!- It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2- oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. -!- It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168. -!- Formerly EC 1.2.4.3.":150,"-!- The enzyme, found in certain soil bacteria and fungi, catalyzes the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. -!- The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination. -!- The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation. -!- Formerly EC 4.1.99.4.":150,"-!- This enzyme has similar activity with either NAD(+) or NADP(+). -!- Cf. EC 1.1.1.118 and EC 1.1.1.119.":150,"1,4-Dihydroxy-2-naphthoyl-CoA synthase":150,"1-aminocyclopropane carboxylic acid deaminase. 1-aminocyclopropane-1-carboxylate endolyase (deaminating). ACC deaminase.":150,"1-aminocyclopropane-1-carboxylate + H(2)O = 2-oxobutanoate + NH(3).":150,"1-aminocyclopropane-1-carboxylate deaminase.":150,"2-hydroxymuconate tautomerase":150,"2-hydroxymuconate tautomerase.":150,"2-oxoisocaproate dehydrogenase. 2-oxoisovalerate (lipoate) dehydrogenase. 3-methyl-2-oxobutanoate dehydrogenase (lipoamide). 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating). Alpha-keto-alpha-methylvalerate dehydrogenase. Alpha-ketoisocaproate dehydrogenase. Alpha-ketoisocaproic dehydrogenase. Alpha-ketoisocaproic-alpha-keto-alpha-methylvaleric dehydrogenase. Alpha-ketoisovalerate dehydrogenase. Alpha-oxoisocaproate dehydrogenase. BCKDH. BCOAD. Branched chain keto acid dehydrogenase. Branched-chain (-2-oxoacid) dehydrogenase (BCD). Branched-chain 2-keto acid dehydrogenase. Branched-chain 2-oxo acid dehydrogenase. Branched-chain alpha-keto acid dehydrogenase. Branched-chain alpha-oxo acid dehydrogenase. Branched-chain keto acid dehydrogenase. Branched-chain ketoacid dehydrogenase. Dehydrogenase, 2-oxoisovalerate (lipoate). Dehydrogenase, branched chain alpha-keto acid.":150,"3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine- residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2).":150,"3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).":150,"4-oxalocrotonate isomerase. 4-oxalocrotonate tautomerase.":150,"5'-D(P*GP*CP*CP*G)-3'":150,"ANTIVIRAL PROTEIN":150,"Agglutinin alpha chain":150,"Anabaena":150,"Arabian camel":150,"Aspergillus terreus":150,"COMPLEMENT FACTOR B":150,"CTD phosphatase activity":150,"Catalytic domain; UNP residues 76-1108":150,"D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H.":150,"DNA (5'-D(*CP*AP*GP*AP*TP*G)-3')":150,"Deleted entry.":150,"Dual specificity mitogen-activated protein kinase kinase 1":150,"Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.":150,"Exomuramidase. Murein lyase F.":150,"Glucose 1-dehydrogenase (NAD(P)(+)).":150,"HEME-AS":150,"IPP isomerase. Isopentenylpyrophosphate Delta-isomerase. Isopentenylpyrophosphate isomerase. Methylbutenylpyrophosphate isomerase.":150,"IgE binding":150,"Isopentenyl diphosphate = dimethylallyl diphosphate.":150,"Isopentenyl-diphosphate Delta-isomerase.":150,"LDHA, PIG19":150,"Leishmania donovani":150,"M17 LEUCYL-AMINOPEPTIDASE, PROTEASE, INHIBITOR, HYDROXAMIC ACID, HYDROLASE-HYDROLASE INHIBITOR complex":150,"MET":150,"METHANOCALDOCOCCUS JANNASCHII":150,"N-glycosylase/DNA lyase":150,"Peptidoglycan lytic exotransglycosylase.":150,"Peptidyl-tRNA hydrolase":150,"Probable M17 family aminopeptidase":150,"RM4018":150,"SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT":150,"Sulfite reductase, dissimilatory-type subunit alpha":150,"TRANSFERASE-TRANSFERASE INHIBITOR complex":150,"Thermobifida fusca":150,"Virion RNA polymerase":150,"alkylbase DNA N-glycosylase activity":150,"betB, SACOL2628":150,"cellular response to interleukin-6":150,"cholesterol catabolic process":150,"dendritic spine morphogenesis":150,"hydrogen peroxide metabolic process":150,"long-term synaptic potentiation":150,"mRNA 5'-UTR binding":150,"monoterpenoid metabolic process":150,"negative regulation of synaptic transmission, GABAergic":150,"nuclear polyadenylation-dependent rRNA catabolic process":150,"phenylethylamine catabolic process":150,"positive regulation of deacetylase activity":150,"potassium channel complex":150,"regulation of ossification":150,"respiratory complex II, inhibitors, Electron transport, Iron, Iron-sulfur, Metal-binding, Mitochondrion, Mitochondrion inner membrane, Oxidoreductase, Transit peptide, Transport, Tricarboxylic acid cycle, Heme, Transmembrane, FAD-binding protein, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex":150,"tt1808, chain A":150,"viral DNA genome packaging":150,"-!- A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines. -!- Is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate. -!- Generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. -!- For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl- 1,2,3,6-tetrahydropyridine (MPTP). -!- Formerly EC 1.13.12.11.":149,"4-{[4-({4-[(E)-2-CYANOETHENYL]-2,6-DIMETHYLPHENYL}AMINO)PYRIMIDIN-2-YL]AMINO}BENZONITRILE":149,"40S ribosomal protein S20":149,"40S ribosomal protein S5":149,"50S RIBOSOMAL PROTEIN L31E":149,"CHLOROPLAST":149,"D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O.":149,"DNA-DIRECTED RNA POLYMERASE II 13.6 KDA POLYPEPTIDE":149,"DNA-DIRECTED RNA POLYMERASES I, II, AND III 14.5 KDA POLYPEPTIDE":149,"DNA-DIRECTED RNA POLYMERASES I, II, AND III 23 KDA POLYPEPTIDE":149,"DNA-DIRECTED RNA POLYMERASES I, II, AND III 27 KDA POLYPEPTIDE":149,"DNA-DIRECTED RNA POLYMERASES I, II, AND III 7.7 KDA POLYPEPTIDE":149,"Dextransucrase.":149,"Dimethylaniline monooxygenase (N-oxide-forming). Dimethylaniline N-oxidase. Dimethylaniline oxidase. DMA oxidase. FAD-containing monooxygenase. Flavin mixed function oxidase. Flavin monooxygenase. FMO. Methylphenyltetrahydropyridine N-monooxygenase. Mixed-function amine oxidase. N,N-dimethylaniline monooxygenase. Ziegler's enzyme.":149,"Elongation factor Ts":149,"Enolase 1":149,"Enterococcus casseliflavus":149,"FE(4)-NI(1)-S(4) CLUSTER":149,"Flavin-containing monooxygenase.":149,"Glucarate dehydratase.":149,"Glutamate decarboxylase beta":149,"Glutamate dehydrogenase 1":149,"Glutaryl-CoA dehydrogenase":149,"Human herpesvirus 4 strain B95-8":149,"Human immunodeficiency virus type 2 (ISOLATE ROD)":149,"Importin subunit alpha-1":149,"Listeria innocua":149,"N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O.":149,"NEDD8 transferase activity":149,"Pol protein":149,"RNA nuclear export complex":149,"Stimulator of interferon genes protein":149,"Sucrose + ((1->6)-alpha-D-glucosyl)(n) = D-fructose + ((1->6)-alpha-D- glucosyl)(n+1).":149,"Sucrose 6-glucosyltransferase.":149,"Transferase, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI":149,"activation of protein kinase A activity":149,"bacterial-type flagellum-dependent swarming motility":149,"cellular response to prostaglandin D stimulus":149,"cyclic-GMP-AMP binding":149,"estradiol 17-beta-dehydrogenase activity":149,"formyltetrahydrofolate dehydrogenase activity":149,"negative regulation of acute inflammatory response":149,"negative regulation of epithelial cell migration":149,"negative regulation of interleukin-17 production":149,"neuronal stem cell population maintenance":149,"oxidative RNA demethylase activity":149,"phosphopantetheine binding":149,"positive regulation of intracellular estrogen receptor signaling pathway":149,"protein kinase activator activity":149,"regulation of transforming growth factor beta receptor signaling pathway":149,"vacuolar membrane":149,"-!- Can modify also synthetic poly(A) and poly(G) to form the structures m(7)G(5')pppAn and m(7)G(5')pppGn.":148,"1-aminocyclopropane-1-carboxylate deaminase":148,"40S ribosomal protein S13":148,"ANTITUMOR PROTEIN":148,"AYE":148,"Beta-lactoglobulin":148,"DNA replication, removal of RNA primer":148,"GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.":148,"GTP--RNA guanylyltransferase. mRNA capping enzyme.":148,"INS":148,"L,D-transpeptidase 2":148,"MEMBRANE PROTEIN/ANTIBIOTIC":148,"OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OXY]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER":148,"PHYLLOQUINONE":148,"PYRUVATE DECARBOXYLASE":148,"Phospho-2-dehydro-3-deoxyheptonate aldolase":148,"RNA splicing, via transesterification reactions":148,"SAM domain binding":148,"Sulfite reductase, dissimilatory-type subunit beta":148,"TGF-beta receptor type-1":148,"TOXOPLASMA GONDII":148,"Transcriptional regulator, TetR family":148,"UDP":148,"VP2":148,"activated T cell proliferation":148,"alpha subunit":148,"chondroitin sulfate catabolic process":148,"culmination involved in sorocarp development":148,"cupric ion binding":148,"death-inducing signaling complex":148,"excretion":148,"glutamine catabolic process":148,"incipient cellular bud site":148,"kinase, TRANSFERASE":148,"leaf development":148,"mRNA guanylyltransferase.":148,"mammary gland epithelial cell differentiation":148,"myeloid dendritic cell differentiation":148,"positive regulation of calcium ion-dependent exocytosis":148,"positive regulation of histone H3-K9 acetylation":148,"response to glucagon":148,"stomatal movement":148,"transsulfuration":148,"turkey":148,"(1) Hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H(2)O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H(+). (2) A [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H(2)O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H(+).":147,"-!- In eukaryotes occurs as a trifunctional enzyme also having EC 1.5.1.5 and EC 3.5.4.9 activity.":147,"-!- The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur- oxidizing bacteria, and organosulfonate reducers. -!- In sulfur reducers it catalyzes the reduction of sulfite to sulfide, while in sulfur oxidizers it catalyzes the opposite reaction. -!- The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. -!- During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC. -!- This disulfide can be reduced by a number of proteins including DsrK and TcmB. -!- This enzyme is different from EC 1.8.1.2 and EC 1.8.7.1, which are involved in sulfate assimilation.":147,"2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHANOL":147,"3-oxoacyl-[acyl-carrier-protein] reductase FabG":147,"7SK snRNA binding":147,"ADENOSINE-5'-MONOPHOSPHATE":147,"ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.":147,"ATPase GET3":147,"Arginine decarboxylase.":147,"Coxsackievirus B3":147,"Dissimilatory sulfite reductase.":147,"Exotoxin A":147,"Ferrous iron transport protein B":147,"Ficolin-2":147,"Formate--tetrahydrofolate ligase.":147,"Formyltetrahydrofolate synthetase. Tetrahydrofolate formylase. Tetrahydrofolic formylase.":147,"GLYCERALDEHYDE-3-PHOSPHATE":147,"GTP cyclohydrolase I":147,"HEME DOMAIN, UNP RESIDUES 297-718":147,"Hexameric":147,"JAK2":147,"L-arginine = agmatine + CO(2).":147,"L-arginine carboxy-lyase.":147,"Lactoperoxidase":147,"Matrix protein 1":147,"Na+,K+-ATPase beta subunit":147,"POL polyprotein":147,"PSEUDOMONAS PHAGE PHI6":147,"Peptide chain release factor 1":147,"Proteinase K":147,"Putative snRNP Sm-like protein":147,"Serine/threonine-protein kinase Chk2":147,"Siroheme sulfite reductase.":147,"Transforming protein RhoA":147,"anterior/posterior axis specification":147,"carnitine biosynthetic process":147,"cellular response to arsenic-containing substance":147,"copper ion transport":147,"cytochrome complex":147,"dendrite membrane":147,"elongation factor G":147,"gonad development":147,"histidine biosynthetic process":147,"lambda repressor-like DNA-binding domains":147,"negative regulation of cell-cell adhesion mediated by cadherin":147,"negative regulation of myeloid cell differentiation":147,"neuropilin binding":147,"nucleocytoplasmic transporter activity":147,"palmitoyltransferase activity":147,"protein methyltransferase activity":147,"pseudouridine synthase activity":147,"regulation of heart rate by cardiac conduction":147,"rhamnose catabolic process":147,"sequence database residues 1-76":147,"sulfurtransferase activity":147,"3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity":146,"40S ribosomal protein S15":146,"700720":146,"Beta-amylase":146,"Chaperonin":146,"Desulfitobacterium hafniense DCB-2":146,"HLA-DQA1":146,"HLA-DRA":146,"ISOMERASE/IMMUNOSUPPRESSANT":146,"Nostoc sp. PCC 7119":146,"POLI, RAD30B":146,"Pck1":146,"Protein recA":146,"Putative alpha-1,2-mannosidase":146,"RHODOBACTER SPHAEROIDES":146,"RIBOSOME, TRANSLATION":146,"RNA helicase activity":146,"SS1":146,"Tyrosine-protein kinase BTK":146,"UDP-glucose 4-epimerase":146,"lactose biosynthetic process":146,"lipoprotein particle":146,"miRNA mediated inhibition of translation":146,"negative regulation of myoblast differentiation":146,"nucleotidyltransferase activity":146,"oxidative single-stranded RNA demethylation":146,"penicillin binding":146,"positive regulation by symbiont of host transcription":146,"positive regulation of ryanodine-sensitive calcium-release channel activity":146,"regulation of endothelial cell migration":146,"ribosomal large subunit binding":146,"ripoptosome":146,"small nucleolar ribonucleoprotein complex":146,"suppression of host defenses":146,"transmembrane receptor protein serine/threonine kinase signaling pathway":146,"(S)-dihydroorotate + a quinone = orotate + a quinol.":145,"-!- Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.":145,"-!- Also acts on benzimidazole, and the clostridial enzyme acts on adenine to form 7-alpha-D-ribosyladenine 5'-phosphate. -!- The product of the reaction, alpha-ribazole 5'-phosphate, forms part of the corrin biosynthesis pathway and is a substrate for EC 2.7.8.2. -!- It can also be dephosphorylated to form alpha-ribazole by the action of EC 3.1.3.73.":145,"-!- From the mold Tritirachium album Limber. -!- Contains two disulfide bridges and one free Cys near the active site His. -!- Belongs to peptidase family S8. -!- Formerly EC 3.4.4.16 and EC 3.4.21.14.":145,"-!- In the presence of NADH and a reductase, 6'-deoxychalcone is produced.":145,"-!- This Class 2 dihydroorotate dehydrogenase enzyme contains FMN. -!- The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane. -!- The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. -!- The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates. -!- Methyl-, ethyl-, tert-butyl and benzyl-(S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not. -!- Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor. -!- Formerly EC 1.3.99.11.":145,"-!- dATP can also act as donor.":145,"20S proteasome, HYDROLASE":145,"3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO(2).":145,"6'-deoxychalcone synthase. Chalcone synthase. Flavonone synthase.":145,"ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.":145,"ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl- tRNA(Gln).":145,"ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+).":145,"ATP-dependent helicase activity":145,"Ac-LAE-ep":145,"Beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate.":145,"CCR5 chemokine receptor binding":145,"CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON SULFUR PROTEIN, CYTOCHROME B, CYTOCHROME C1, COMPLEX III, MITOCHONDRIAL PROCESSING PROTEIN, UBIQUINONE, AZOXYSTROBIN OXIDOREDUCTASE, REDOX ENZYME RESPIRATORY CHAIN, ELECTRON TRANSPORT, HEME, INNER MEMBRANE, MEMBRANE, STROBILURINS BINDING, MITOCHONDRION, TRANSMEMBRANE, STIGMATELLIN, IRON, MITOCHONDRIAL INNER MEMBRANE, RESPIRATORY CHAIN, IRON-SULFUR, TRANSIT PEPTIDE, Metal-binding, Mitochondrion inner membrane, Transport, Disulfide bond, OXIDOREDUCTASE":145,"Catabolite gene activator":145,"Chlorobaculum tepidum":145,"DHOD. DHOdehase. DHODH.":145,"DNA (5'-D(*CP*AP*TP*CP*TP*GP*T)-3')":145,"Deamido-NAD(+) diphosphorylase. Deamido-NAD(+) pyrophosphorylase.":145,"Dihydroorotate dehydrogenase (quinone).":145,"Dihydropteroate synthase":145,"Endopeptidase K. Proteinase K. Tritirachium album proteinase K. Tritirachium alkaline proteinase.":145,"GNG2":145,"GTP CYCLOHYDROLASE I":145,"Glutamate racemase":145,"Glutamine translase. Glutaminyl-tRNA synthetase.":145,"Glutamine--tRNA ligase.":145,"HIST1H3A, H3FA, HIST1H3B, H3FL, HIST1H3C, H3FC, HIST1H3D, H3FB, HIST1H3E, H3FD, HIST1H3F, H3FI, HIST1H3G, H3FH, HIST1H3H, H3FK, HIST1H3I, H3FF, HIST1H3J, H3FJ":145,"HYDROLASE complex, Proteasome, Mutant, Binding Analysis, HYDROLASE-HYDROLASE INHIBITOR complex":145,"Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.":145,"Igh protein":145,"Malic enzyme. NAD-malic enzyme. Pyruvic-malic carboxylase.":145,"N(1)-alpha-phosphoribosyltransferase. Nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase.":145,"Naringenin-chalcone synthase.":145,"Nicotinate-nucleotide adenylyltransferase.":145,"Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase.":145,"Norovirus Hu/1968/US":145,"PAD.":145,"PROTEASOME SUBUNIT ALPHA TYPE-1":145,"PROTEASOME SUBUNIT ALPHA TYPE-2":145,"PROTEASOME SUBUNIT ALPHA TYPE-3":145,"PROTEASOME SUBUNIT ALPHA TYPE-4":145,"PROTEASOME SUBUNIT ALPHA TYPE-5":145,"PROTEASOME SUBUNIT ALPHA TYPE-6":145,"PROTEASOME SUBUNIT BETA TYPE-2":145,"PROTEASOME SUBUNIT BETA TYPE-3":145,"PROTEASOME SUBUNIT BETA TYPE-4":145,"PROTEASOME SUBUNIT BETA TYPE-6":145,"PROTEASOME SUBUNIT BETA TYPE-7":145,"PTERIDINE REDUCTASE 1":145,"Parengyodontium album":145,"Peptidase K.":145,"Phosphoribosyl diphosphate synthetase. Phosphoribosyl pyrophosphate synthetase. Ribose-phosphate pyrophosphokinase.":145,"Proteasome, Epoxyketone, Immunoproteasome Inhibitor, Binding Analysis, HYDROLASE-HYDROLASE INHIBITOR complex":145,"Protein L-arginine + H(2)O = protein L-citrulline + NH(3).":145,"Protein-arginine deiminase.":145,"RNA stem-loop binding":145,"Ribose-phosphate diphosphokinase.":145,"SPIRILLOXANTHIN":145,"Schmidt-Lanterman incisure":145,"Streptococcus agalactiae NEM316":145,"adenylate cyclase-activating G-protein coupled receptor signaling pathway":145,"cellular response to macrophage colony-stimulating factor stimulus":145,"cochlea development":145,"high-density lipoprotein particle assembly":145,"intrinsic component of membrane":145,"iron storage protein, disorder, Iron, Iron storage, Metal-binding":145,"late endosome to vacuole transport via multivesicular body sorting pathway":145,"negative regulation of RNA interference":145,"negative regulation of cytokine secretion involved in immune response":145,"negative regulation of interleukin-2 biosynthetic process":145,"negative regulation of receptor-mediated endocytosis":145,"pentose-phosphate shunt, non-oxidative branch":145,"phosphatidylinositol-3,5-bisphosphate binding":145,"protein localization to nucleolus":145,"regulation of B cell cytokine production":145,"sequence database residues 77-272":145,"viral procapsid":145,"(S)-mandelate = (R)-mandelate.":144,"-!- From the bacterium Bacilus anthracis that causes anthrax. -!- One of three proteins that are collectively termed anthrax toxin. -!- Cleaves several MAP kinase kinases near their N-termini, preventing them from phosphorylating the downstream mitogen-activated protein kinases. -!- Belongs to peptidase family M34.":144,"-!- Responsible for the post-translational processing of the human immunodeficiency virus polyprotein. -!- Belongs to peptidase family A2.":144,"60S RIBOSOMAL PROTEIN L9":144,"Anthrax lethal factor endopeptidase.":144,"Arginine repressor":144,"Arthrobacter sp.":144,"CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL":144,"Carbon monoxide dehydrogenase medium chain":144,"Cryptosporidium hominis":144,"DNA (5'-D(*AP*TP*TP*GP*TP*CP*AP*TP*GP*GP*AP*AP*TP*TP*TP*CP*GP*CP*A)-3')":144,"DNA binding protein":144,"Endopeptidase for which the P1 residue is preferably hydrophobic.":144,"Glutamate receptor ionotropic, NMDA 1":144,"Golgi-associated vesicle membrane":144,"HIV-2 retropepsin.":144,"Human rhinovirus B":144,"Insulin receptor":144,"Lethal toxin.":144,"Mandelate racemase.":144,"Ornithine carbamoyltransferase":144,"POL POLYPROTEIN":144,"PYK":144,"Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.":144,"Proteasome (Alpha subunit) PrcA":144,"Proteasome (Beta subunit) PrcB":144,"UNP residues 144-1102":144,"VANILLYL-ALCOHOL OXIDASE":144,"W83":144,"aldehyde dehydrogenase (NADP+) activity":144,"anaphase-promoting complex":144,"branching involved in blood vessel morphogenesis":144,"calcium-release channel activity":144,"camC, cyp101":144,"clathrin heavy chain binding":144,"entrainment of circadian clock by photoperiod":144,"fatty acid beta-oxidation using acyl-CoA dehydrogenase":144,"mitotic nuclear envelope reassembly":144,"negative regulation of osteoblast differentiation":144,"positive regulation of histone phosphorylation":144,"prcA, Rv2109c":144,"regulation of neuron migration":144,"signal transduction involved in intra-S DNA damage checkpoint":144,"(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID":143,"-!- Generally membrane bound enzyme present in both mammalian and bacterial cells. -!- Belongs to peptidase family M24B.":143,"A-SITE TRNA G24A TRP-TRNA TRP":143,"Achromobacter cycloclastes":143,"Aminoacylproline aminopeptidase. Aminopeptidase P. Proline aminopeptidase. X-Pro aminopeptidase.":143,"CMCP6":143,"Conserved protein":143,"DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE":143,"DNA-3-methyladenine glycosylase 2":143,"Dioxygenase, 2-His-1-carboxylate facial triad, oxygen activation, acid-base catalysis, Oxidoreductase":143,"Fab, heavy chain":143,"Fab, light chain":143,"Glutamine--tRNA ligase":143,"KINASE DOMAIN":143,"PHOSPHITE ION":143,"Prkaca, Pkaca":143,"Protein S100-B":143,"RIMD 2210633":143,"Rd KW20":143,"Recombinase cre":143,"Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.":143,"Salmonella typhimurium LT2":143,"Synechocystis sp. PCC 6803":143,"TOR signaling":143,"Trypanosoma cruzi (strain CL Brener)":143,"VIRAL PROTEIN/RNA":143,"Xaa-Pro aminopeptidase.":143,"cellular response to inorganic substance":143,"deoxyribonuclease activity":143,"dephosphorylation of RNA polymerase II C-terminal domain":143,"glutamine metabolic process":143,"positive regulation of cholesterol efflux":143,"shelterin complex":143,"soybeans":143,"sphingolipid biosynthetic process":143,"succinate-CoA ligase complex (ADP-forming)":143,"sulfate assimilation":143,"vascular endothelial growth factor receptor 1 binding":143,"zf-C2H2, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, TRANSCRIPTION":143,"-!- Forms part of the purine biosynthesis pathway.":142,"4-((N-succinylamino)carbonyl)-5-aminoimidazole ribonucleotide synthetase. 4-(N-succinocarboxamide)-5-aminoimidazole synthetase. 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase. Phosphoribosylaminoimidazole-succinocarboxamide synthase. Phosphoribosylaminoimidazole-succinocarboxamide synthetase. Phosphoribosylaminoimidazolesuccinocarboxamide synthetase. SAICAR synthase. SAICAR synthetase. SAICARs.":142,"AIM2 inflammasome complex":142,"ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate.":142,"BACILLUS ANTHRACIS":142,"Carboxydothermus hydrogenoformans Z-2901":142,"Cytochrome b-c1 complex subunit 8":142,"D-alanine catabolic process":142,"Dengue virus 2":142,"HB27 / ATCC BAA-163 / DSM 7039":142,"HLH, helix-loop-helix DNA-binding domain":142,"Nuclease A (UNP residues 83-231)":142,"PCNA complex":142,"PUTATIVE ALPHA-1,2-MANNOSIDASE":142,"Phosphoribosylaminoimidazolesuccinocarboxamide synthase.":142,"Photoactive yellow protein":142,"Protein argonaute-2":142,"Pseudomonas pseudomallei":142,"RESIDUES 20-755":142,"SCF complex assembly":142,"UMP biosynthetic process":142,"Unconventional myosin-VI":142,"Xanthomonas oryzae pv. oryzae KACC 10331":142,"acetolactate synthase activity":142,"brush border membrane":142,"cullin family protein binding":142,"histone deacetylase regulator activity":142,"interleukin-18-mediated signaling pathway":142,"low-density lipoprotein receptor activity":142,"lymphocyte aggregation":142,"lysine biosynthetic process via diaminopimelate":142,"methylglyoxal metabolic process":142,"positive regulation of Wnt signaling pathway, planar cell polarity pathway":142,"positive regulation of fatty acid beta-oxidation":142,"pre-mRNA binding":142,"regulation of RNA splicing":142,"regulation of protein ADP-ribosylation":142,"transforming growth factor beta receptor activity, type I":142,"-!- Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. -!- The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. -!- Cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3- tricarboxylate. -!- Formerly EC 4.2.1.4.":141,"-!- Catalyzes the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. -!- Does not act on acetylated mannan or pectin.":141,"-!- The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7.":141,"5'-R(*UP*UP*CP*GP*AP*CP*CP*AP*GP*GP*AP)-3'":141,"A/Puerto Rico/8/1934 H1N1":141,"ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.":141,"Abu_1752":141,"Acetylxylan esterase.":141,"Aconitase. Cis-aconitase. Citrate hydro-lyase. Citrate(isocitrate) hydro-lyase.":141,"Aconitate hydratase.":141,"Arcobacter butzleri":141,"Bergmann glial cell differentiation":141,"CD1D":141,"CG10419":141,"Calmodulin-domain protein kinase 1":141,"Citrate = isocitrate.":141,"Complex, Assembly Machinery, SPLICING":141,"DNA joinase. DNA repair enzyme. Polydeoxyribonucleotide synthase (ATP). Polynucleotide ligase (ATP). Sealase.":141,"DNA ligase (ATP).":141,"Deacetylation of xylans and xylo-oligosaccharides.":141,"Dmel_CG4924, icln, icln-RA":141,"Ferrochelatase, mitochondrial":141,"Formate--tetrahydrofolate ligase":141,"Fructose-bisphosphate aldolase":141,"Gem2, CG10419, Dmel_CG10419":141,"Glyceraldehyde-3-phosphate dehydrogenase 1":141,"Icln":141,"JC polyomavirus":141,"LD23602p":141,"MANGANESE (III) ION":141,"Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein":141,"Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c":141,"Molybdopterin molybdenumtransferase":141,"Moorella thermoacetica ATCC 39073":141,"NAD biosynthetic process":141,"Nitroalkane oxidase":141,"Psophocarpus tetragonolobus":141,"Smn, CG16725, Dmel_CG16725":141,"Tankyrase-1":141,"Thioredoxin reductase":141,"UNP residues 1-122":141,"VP3":141,"azu, PA4922":141,"beta subunit":141,"central nervous system morphogenesis":141,"exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)":141,"mating projection tip":141,"micro-ribonucleoprotein complex":141,"molybdenum incorporation into molybdenum-molybdopterin complex":141,"negative regulation of lipase activity":141,"negative regulation of protein acetylation":141,"nirK, nir":141,"nuclear polyadenylation-dependent tRNA catabolic process":141,"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen":141,"peptide deformylase activity":141,"polytene chromosome":141,"positive regulation of pseudopodium assembly":141,"pufM":141,"root development":141,"transcription coactivator binding":141,"vesicle transport along microtubule":141,"(1) (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. (2) Oxaloacetate = pyruvate + CO(2).":140,"(1) An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H(2)O = a [protein]-L-arginine + (R)-lactate. (2) An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + (R)-lactate. (3) An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H(2)O = a [protein]-L-cysteine + (R)-lactate.":140,"-!- Also acts with L-aspartate and, more slowly, with some other amino acids.":140,"-!- Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors.":140,"-!- Possibly thiol dependent. -!- Cytosolic from most animal tissues. -!- Belongs to peptidase family M24A. -!- Formerly EC 3.4.3.7.":140,"-!- The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. -!- The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. -!- The enzyme repairs the amino acids, releasing glycolate or (R)- lactate, depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively.":140,"-!- Unlike EC 1.1.1.39, this enzyme can also decarboxylate oxaloacetate, cf. EC 1.1.1.40.":140,"2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.":140,"3D":140,"ATP-grasp fold, B domain":140,"Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.":140,"Amino-acid N-acetyltransferase.":140,"Argininosuccinate lyase":140,"Argininosuccinate lyase.":140,"Arginosuccinase. N-(L-argininosuccinate) arginine-lyase. Omega-N-(L-arginino)succinate arginine-lyase.":140,"Bacteroides vulgatus":140,"CORE":140,"Cytochrome b-c1 complex subunit 9":140,"D-XYLOSE ISOMERASE":140,"D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = 3-phospho-D- glyceroyl phosphate + NADPH.":140,"DNA replication origin binding":140,"Deoxycytidine kinase":140,"Deoxycytidine kinase.":140,"Dntt, Tdt":140,"FARNESYL DIPHOSPHATE":140,"GNB1":140,"Gamma-peptidase. Imidodipeptidase. Peptidase D. Prolidase. Proline dipeptidase. X-Pro dipeptidase.":140,"Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating).":140,"Golgi stack":140,"Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2":140,"H-2 class II histocompatibility antigen, E-K alpha chain":140,"HCK":140,"Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.":140,"Inositol 2-dehydrogenase.":140,"MB":140,"MEMBRANE PROTEIN, ION PUMP, ATPASE, K+ BINDING, HALOACID DEHYDROGENEASE SUPERFAMILY, PHOSPHATE ANALOGUE, ATP-BINDING, HYDROLASE, ION TRANSPORT, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, HYDROLASE-TRANSPORT PROTEIN COMPLEX, KINETICS":140,"Malate dehydrogenase (oxaloacetate-decarboxylating).":140,"Myo-inositol + NAD(+) = 2,4,6/3,5-pentahydroxycyclohexanone + NADH.":140,"Myo-inositol 2-dehydrogenase.":140,"N-acetylglutamate synthase.":140,"NADP-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase (NADP(+)). Triosephosphate dehydrogenase (NADP+).":140,"NTP + deoxycytidine = NDP + dCMP.":140,"PROTEASE RETROPEPSIN":140,"Protein deglycase.":140,"RV-A":140,"SMAD protein signal transduction":140,"Structural Protein":140,"TRANSCRIPTION/RNA":140,"TRANSFERASE/CELL CYCLE":140,"Xaa-Pro dipeptidase.":140,"anion binding":140,"apicolateral plasma membrane":140,"arginine deiminase pathway":140,"blood vessel morphogenesis":140,"carboxylic ester hydrolase activity":140,"chemokine-mediated signaling pathway":140,"deoxycytidine kinase activity":140,"establishment of protein localization to chromatin":140,"fumarate hydratase activity":140,"negative regulation of gluconeogenesis":140,"negative regulation of receptor internalization":140,"nuclear pore outer ring":140,"palate development":140,"positive regulation of cytokine secretion involved in immune response":140,"positive regulation of interleukin-13 production":140,"positive regulation of metallopeptidase activity":140,"protein adenylylation":140,"protein-arginine omega-N monomethyltransferase activity":140,"regulation of proteolysis":140,"-!- Phenazine methosulfate can act as acceptor. -!- Acts on aromatic amines and, more slowly, on some long-chain aliphatic amines, but not on methylamine or ethylamine. -!- Formerly EC 1.4.99.4.":139,"-!- The enzyme preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates. -!- In vitro the enzyme also acts as a nucleotidohydrolase on ADP, NAD(+), NADP(+), FAD, and CoA. -!- Formerly EC 3.6.1.19.":139,"-!- This prokaryotic enzyme catalyzes the reversible reduction of CO(2) to CO. -!- The electrons are transferred to redox proteins such as ferredoxin. -!- In purple sulfur bacteria and methanogenic archaea it catalyzes the oxidation of CO to CO(2), which is incorporated by the Calvin-Benson- Basham cycle or released, respectively. -!- In acetogenic and sulfate-reducing microbes it catalyzes the reduction of CO(2) to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, with which the enzyme forms a tight complex in those organisms. -!- In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2 which catalyze the overall reaction: CO + H(2)O = CO(2) + H(2). -!- Cf. EC 1.2.5.3. -!- Formerly EC 1.2.99.2.":139,"A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate.":139,"ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H":139,"ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).":139,"Alkyl hydroperoxide reductase AhpD":139,"Anaerobic carbon-monoxide dehydrogenase.":139,"ArCH(2)NH(2) + H(2)O + 2 azurin = ArCHO + NH(3) + 2 reduced azurin.":139,"Aralkylamine dehydrogenase (azurin).":139,"Aromatic amine dehydrogenase. Arylamine dehydrogenase.":139,"Aspartate--tRNA ligase.":139,"Aspartic acid translase. Aspartyl-tRNA synthetase.":139,"Beta-mannosidase":139,"Borrelia":139,"Branched-chain-amino-acid aminotransferase, mitochondrial":139,"CO + H(2)O + 2 oxidized ferredoxin = CO(2) + 2 reduced ferredoxin + 2 H(+).":139,"Carbon-monoxide dehydrogenase (ferredoxin). Ni-CODH.":139,"Chloroflexus aurantiacus J-10-fl":139,"Cytochrome c'":139,"Cytosolic 10-formyltetrahydrofolate dehydrogenase":139,"DNA (5'-D(*CP*AP*GP*TP*AP*C)-3')":139,"DNA-directed RNA polymerase II 14.2 kDa polypeptide":139,"Dinucleotide nucleotidohydrolase. Nucleoside-triphosphate diphosphatase. Nucleotide pyrophosphatase.":139,"ENDOTHELIAL":139,"FGA":139,"Glycosidases":139,"HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex":139,"Human rhinovirus 14":139,"Kinesin-like protein KIF11":139,"L-METHIONINE-S-SULFOXIMINE PHOSPHATE":139,"Mycobacterium avium subsp. paratuberculosis K-10":139,"Nucleotide diphosphatase.":139,"P granule":139,"REVERSE TRANSCRIPTASE/RIBONUCLEASE H":139,"SAMARIUM (III) ION":139,"SH2 DOMAIN":139,"Single-stranded DNA-binding protein":139,"UNP residues 1-373":139,"V-type ATP synthase alpha chain":139,"[Clostridium] symbiosum":139,"caspase binding":139,"centrosome localization":139,"chloroplast thylakoid":139,"detection of calcium ion":139,"dnaX, dnaZ, dnaZX, b0470, JW0459":139,"farnesol catabolic process":139,"geranylgeranyl reductase activity":139,"holA, b0640, JW0635":139,"holB, b1099, JW1085":139,"hydrogen sulfide biosynthetic process":139,"intrinsic component of the cytoplasmic side of the plasma membrane":139,"mRNA cleavage involved in gene silencing by miRNA":139,"methionine metabolic process":139,"regulation of protein secretion":139,"sequestering of triglyceride":139,"viral budding":139,"1-pyrroline-5-carboxylate dehydrogenase":138,"2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase":138,"60S RIBOSOMAL PROTEIN L27A":138,"ATP-dependent protease subunit HslV":138,"Beta-xylosidase":138,"Bromodomain-containing protein 2":138,"Carbon monoxide dehydrogenase small chain":138,"Caulobacter vibrioides":138,"Divalent-cation tolerance protein CutA":138,"Emericella nidulans":138,"FACTOR X LIGHT CHAIN":138,"FDPS, FPS, KIAA1293":138,"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2":138,"Kinase Domain":138,"LIGHT CHAIN":138,"Mycothermus thermophilus":138,"NAD kinase 1":138,"Phosphoribosylaminoimidazole-succinocarboxamide synthase":138,"Pyranose 2-oxidase":138,"Ribose-5-phosphate isomerase A":138,"SIGNALING PROTEIN,TRANSFERASE":138,"Streptomyces lavendulae":138,"Transcription Factor, Ets-1":138,"activation of MAPKKK activity":138,"aspartate metabolic process":138,"camera-type eye development":138,"demethylation":138,"extracellular structure organization":138,"histone H3-R26 citrullination":138,"hydrogenase (acceptor) activity":138,"immunoglobulin fold, IMMUNE SYSTEM":138,"iron-cytochrome-c reductase activity":138,"negative regulation of endoplasmic reticulum unfolded protein response":138,"negative regulation of epithelial to mesenchymal transition":138,"negative regulation of interleukin-2 production":138,"nitrate catabolic process":138,"oxidoreductase activity, acting on phosphorus or arsenic in donors":138,"phagocytic cup":138,"positive regulation of histone deacetylase activity":138,"positive regulation of multicellular organism growth":138,"positive regulation of steroid hormone biosynthetic process":138,"positive regulation of transforming growth factor beta production":138,"protein citrullination":138,"protein-arginine deiminase activity":138,"proton transport":138,"pyramidal neuron migration":138,"sulfotransferase activity":138,"(2AE,4E,5'S,6S,6'R,7S,8E,11R,13R,15S,17AR,20R,20AR,20BS)-6'-[(2S)-BUTAN-2-YL]-20,20B-DIHYDROXY-5',6,8,19-TETRAMETHYL-17-OXO-3',4',5',6,6',10,11,14,15,17,17A,20,20A,20B-TETRADECAHYDRO-2H,7H-SPIRO[11,15-METHANOFURO[4,3,2-PQ][2,6]BENZODIOXACYCLOOCTADECINE-13,2'-PYRAN]-7-YL 2,6-DIDEOXY-4-O-(2,6-DIDEOXY-3-O-METHYL-ALPHA-L-ARABINO-HEXOPYRANOSYL)-3-O-METHYL-ALPHA-L-ARABINO-HEXOPYRANOSIDE":137,"235aa long hypothetical biotin--[acetyl-CoA-carboxylase] ligase":137,"3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL":137,"35092":137,"40S RIBOSOMAL PROTEIN RACK1":137,"Acinetobacter":137,"Acting on carbon-nitrogen bonds, other than peptide bonds.":137,"Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1":137,"Antibody heavy chain":137,"Antibody light chain":137,"Carbon--nitrogen ligases with glutamine as amido-N-donor.":137,"Cd1.1, CD1d, Cd1d1":137,"DC3000":137,"DLD, GCSL, LAD, PHE3":137,"DNA polymerase III, clamp loader complex":137,"Dihydroorotate dehydrogenase (quinone), mitochondrial":137,"ENTEROCOCCUS FAECALIS":137,"FE4-S3 CLUSTER":137,"FGB":137,"FLAVODOXIN":137,"Fab fragment":137,"Fatty acid synthase":137,"HTH-type transcriptional regulator qacR":137,"Hepatitis C virus (isolate H)":137,"L-rhamnose isomerase":137,"L-serine catabolic process":137,"Meleagris":137,"N-FORMYLMETHIONINE":137,"NADH-quinone oxidoreductase subunit 1":137,"NEDD8-activating enzyme E1 catalytic subunit":137,"Paenarthrobacter aurescens TC1":137,"Proteasome subunit beta type-8":137,"Putative ferritin homolog":137,"Receptor tyrosine-protein kinase erbB-2":137,"S2":137,"SAMHD1, MOP5":137,"Streptococcus thermophilus LMG 18311":137,"TRANSFERASE, STRUCTURE BASED DRUG DESIGN":137,"UNIDENTIFIED":137,"Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial":137,"Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial":137,"cell-cell junction assembly":137,"glycine metabolic process":137,"intracellular ferritin complex":137,"isolate 3D7":137,"negative regulation of activated T cell proliferation":137,"negative regulation of core promoter binding":137,"positive regulation of androgen receptor activity":137,"positive regulation of receptor recycling":137,"posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery":137,"regulation of cell cycle arrest":137,"regulation of neuron differentiation":137,"regulation of vacuole fusion, non-autophagic":137,"salivary gland cell autophagic cell death":137,"skin development":137,"1-deoxy-1-({2,6-dioxo-5-[(E)-(2-oxopropylidene)amino]-1,2,3,6-tetrahydropyrimidin-4-yl}amino)-D-ribitol":136,"ALDH2 OR ALDM":136,"ATCC 19977 / DSM 44196":136,"ATCC BAA-535 / M":136,"Acetoanaerobium sticklandii DSM 519":136,"BETA-SECRETASE 1":136,"Capsid protein VP3":136,"Catabolite control protein A":136,"Clostridium beijerinckii":136,"Complete mature sequence (does not contain mitochondrial leader sequence).":136,"DARPin":136,"Encephalitozoon cuniculi GB-M1":136,"Endodeoxyribonucleases producing 5'-phosphomonoesters.":136,"GAMMA-AMINO-BUTANOIC ACID":136,"Galectin-1":136,"Glutaminase kidney isoform, mitochondrial":136,"Human immunodeficiency virus type 1 (isolate YU2)":136,"INORGANIC PYROPHOSPHATASE":136,"Immunoglobulin kappa constant":136,"LAMA GLAMA":136,"Moloney murine leukemia virus isolate Shinnick":136,"Monoclonal antibody 10E5 heavy chain":136,"Monoclonal antibody 10E5 light chain":136,"NEURAMINIDASE":136,"Nostoc punctiforme PCC 73102":136,"Oligotropha carboxidovorans OM5":136,"Rhodnius":136,"SPECTINOMYCIN":136,"Sialidase":136,"TRANSCRIPTION, MRNA, MULTIPROTEIN COMPLEX, MOLECULAR MACHINE, ZINC MOTIFS":136,"UCBPP-PA14":136,"Xanthomonas campestris":136,"bile acid biosynthetic process":136,"cAMP-dependent protein kinase inhibitor alpha":136,"calcium channel regulator activity":136,"cell fate specification":136,"cellular carbohydrate metabolic process":136,"embryonic pattern specification":136,"fatty acid beta-oxidation using acyl-CoA oxidase":136,"hexokinase activity":136,"insulin secretion":136,"mRNA cleavage factor complex":136,"mitotic spindle pole body":136,"negative regulation of low-density lipoprotein particle receptor catabolic process":136,"nitrite reductase (NO-forming) activity":136,"nuclear stress granule":136,"oxidoreductase activity, acting on peroxide as acceptor":136,"peptidyl-lysine acetylation":136,"positive regulation of B cell activation":136,"positive regulation of core promoter binding":136,"posttranscriptional gene silencing by RNA":136,"signal sequence binding":136,"translocation of peptides or proteins into host cell cytoplasm":136,"triphosphatase activity":136,"ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway":136,"vascular endothelial growth factor receptor binding":136,"-!- Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3, EC 4.3.1.24 and EC 4.3.1.25. -!- Far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides. -!- Formerly EC 4.3.1.5.":135,"-!- The flavin is both covalently and non-covalently bound in a molar ratio of 1:1.":135,"146-MER DNA":135,"ATP synthase subunit delta, mitochondrial":135,"ATP-dependent Clp protease proteolytic subunit 1":135,"Actin-related protein 2":135,"BIS(ADENOSINE)-5'-PENTAPHOSPHATE":135,"Cadherin-1":135,"Camelus":135,"D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2- oxopropyl phosphate + H(2)O.":135,"FATTY ACID SYNTHASE BETA SUBUNITS":135,"Fructose-bisphosphate aldolase A":135,"GLYCOGEN PHOSPHORYLASE":135,"Glutamyl-tRNA(Gln) amidotransferase subunit C":135,"H2-Aa":135,"Imidazoleglycerol-phosphate dehydratase.":135,"Immunoglobulin heavy constant epsilon":135,"L-tyrosine = trans-p-hydroxycinnamate + ammonia.":135,"L-tyrosine ammonia-lyase. TAL. Tyrase.":135,"Light Chain":135,"Ovomucoid":135,"PROTOPORPHYRIN IX CONTAINING CO":135,"Phosphatidylinositol 3-kinase regulatory subunit alpha":135,"Photosynthetic reaction center M subunit":135,"Pseudo-nitzschia multiseries":135,"SUGAR (BETA-CYCLODEXTRIN)":135,"Sarcosine + H(2)O + O(2) = glycine + formaldehyde + H(2)O(2).":135,"Sarcosine oxidase.":135,"Silicibacter pomeroyi":135,"Spectrin alpha chain, non-erythrocytic 1":135,"Sphaerobacter thermophilus DSM 20745":135,"TRICLOSAN":135,"Transferring other groups.":135,"Tyrosine ammonia-lyase.":135,"arginine catabolic process to ornithine":135,"bullfrogs":135,"capsule":135,"carnitine shuttle":135,"chromosome condensation":135,"collagen biosynthetic process":135,"enhancer sequence-specific DNA binding":135,"estrogen biosynthetic process":135,"gastrulation":135,"heterocycle metabolic process":135,"ion channel complex":135,"negative regulation of growth":135,"netrin-activated signaling pathway":135,"nitrate transport":135,"nitric oxide binding":135,"positive regulation of alkaline phosphatase activity":135,"purine nucleoside catabolic process":135,"regulation of L-arginine import":135,"regulation of substrate adhesion-dependent cell spreading":135,"single-stranded DNA 3'-5' exodeoxyribonuclease activity":135,"transketolase activity":135,"tyrosine ammonia-lyase activity":135,"vinculin binding":135,"-!- Also acts on 5'-deoxyadenosine and other analogs having 5'-deoxy groups.":134,"-!- Inhibited by pepstatin. -!- Belongs to peptidase family A1.":134,"-!- Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. -!- Activity is stimulated by certain phospholipids. -!- In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. -!- cf. EC 2.7.1.174.":134,"2',3'-DIDEOXY-THYMIDINE-5'-TRIPHOSPHATE":134,"40S RIBOSOMAL PROTEIN RPS10E":134,"40S RIBOSOMAL PROTEIN RPS11E":134,"40S RIBOSOMAL PROTEIN RPS12E":134,"40S RIBOSOMAL PROTEIN RPS13E":134,"40S RIBOSOMAL PROTEIN RPS14E":134,"40S RIBOSOMAL PROTEIN RPS15E":134,"40S RIBOSOMAL PROTEIN RPS16E":134,"40S RIBOSOMAL PROTEIN RPS17E":134,"40S RIBOSOMAL PROTEIN RPS18E":134,"40S RIBOSOMAL PROTEIN RPS19E":134,"40S RIBOSOMAL PROTEIN RPS20E":134,"40S RIBOSOMAL PROTEIN RPS21E":134,"40S RIBOSOMAL PROTEIN RPS22E":134,"40S RIBOSOMAL PROTEIN RPS25E":134,"40S RIBOSOMAL PROTEIN RPS26E":134,"40S RIBOSOMAL PROTEIN RPS28E":134,"40S RIBOSOMAL PROTEIN RPS29E":134,"40S RIBOSOMAL PROTEIN RPS2E":134,"40S RIBOSOMAL PROTEIN RPS30E":134,"40S RIBOSOMAL PROTEIN RPS31E":134,"40S RIBOSOMAL PROTEIN RPS3E":134,"40S RIBOSOMAL PROTEIN RPS4E":134,"40S RIBOSOMAL PROTEIN RPS5E":134,"40S RIBOSOMAL PROTEIN RPS9E":134,"47085":134,"5'-deoxy-5'-methylthioadenosine phosphorylase. 5'-methylthioadenosine phosphorylase. MeSAdo phosphorylase. MeSAdo/Ado phosphorylase. Methylthioadenosine nucleoside phosphorylase. Methylthioadenosine phosphorylase. MTA phosphorylase. MTAPase.":134,"70S, Ribosome, Translation, Peptydil Transfer Reaction, Proton Transfer Mechanism, Acylated tRNA":134,"ACTIVATED FACTOR XA HEAVY CHAIN":134,"ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.":134,"Acting on other nitrogenous compounds as donors.":134,"Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3":134,"Avidin":134,"Beta-adrenergic receptor kinase 1":134,"D-mannonate dehydratase":134,"DCK":134,"DGK. Diglyceride kinase.":134,"Death Domain, Fas":134,"Delta-aminolevulinic acid dehydratase":134,"Diacylglycerol kinase (ATP).":134,"FTN":134,"Fusion glycoprotein F0":134,"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]":134,"Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic":134,"IRAK4":134,"Influenza A virus (A/Shanghai/02/2013(H7N9))":134,"O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL":134,"PCSK9-AnxA2 complex":134,"PIN1":134,"Photosynthetic reaction center H subunit":134,"Photosynthetic reaction center L subunit":134,"Polb":134,"Pyrroline-5-carboxylate reductase":134,"RSA493":134,"Ribosomal protein es25":134,"Ribosomal protein uS11":134,"Ribosomal protein uS12":134,"S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha- D-ribose 1-phosphate.":134,"S-methyl-5'-thioadenosine phosphorylase":134,"S-methyl-5'-thioadenosine phosphorylase.":134,"SB210":134,"TRANSLATION INITIATION FACTOR EIF-1A FAMILY PROTEIN":134,"UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate.":134,"UMP diphosphorylase. UMP pyrophosphorylase.":134,"Uracil phosphoribosyltransferase.":134,"basophil chemotaxis":134,"calcium ion homeostasis":134,"cellular response to menadione":134,"exoribonuclease activity":134,"negative regulation of cardiac muscle cell proliferation":134,"nerve growth factor processing":134,"nuclease activity":134,"oxidized purine nucleobase lesion DNA N-glycosylase activity":134,"positive regulation of T cell apoptotic process":134,"positive regulation of peptidyl-tyrosine autophosphorylation":134,"positive regulation of protein kinase D signaling":134,"potassium ion import across plasma membrane":134,"pre-mRNA cleavage required for polyadenylation":134,"regulation of DNA replication":134,"regulation of cell growth":134,"solute:proton antiporter activity":134,"telomeric D-loop disassembly":134,"vascular endothelial growth factor signaling pathway":134,"-!- The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products. -!- Formerly EC 4.6.1.3.":133,"-!- Up-regulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment. -!- Can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP). -!- Belongs to peptidase family S1B.":133,"2-aminomuconate 6-semialdehyde dehydrogenase":133,"3-dehydroquinate synthase.":133,"3-dehydroquinate synthetase. 5-dehydroquinate synthase. 5-dehydroquinic acid synthetase. Dehydroquinate synthase.":133,"3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.":133,"ALPHA D-GALACTOSE":133,"ALPHA-LYTIC PROTEASE":133,"ATCC 14579 / DSM 31":133,"Acting on carbohydrates and derivatives.":133,"Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase":133,"CSBP, CSBP1, CSBP2, CSPB1, MAPK14, MXI2":133,"Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.":133,"CoA hydrolase activity":133,"D-serine catabolic process":133,"Elongation factor Tu":133,"Fatty acid synthase subunit beta":133,"GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE":133,"GREAT POND SNAIL":133,"HEN EGG WHITE LYSOZYME":133,"HLA class I histocompatibility antigen, B-27 alpha chain":133,"High temperature requirement protein A2. HtrA2 protease. Omi stress-regulated endoprotease. Serine proteinase OMI.":133,"HtrA2 peptidase.":133,"Iowa II":133,"LYMNAEA STAGNALIS":133,"Leptospira interrogans serovar Lai str. 56601":133,"Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase":133,"Propionibacterium":133,"Protein farnesyltransferase subunit beta":133,"RNA phosphodiester bond hydrolysis, endonucleolytic":133,"SN-GLYCEROL-3-PHOSPHATE":133,"SUCROSE":133,"SUGAR (GALACTOSE-URIDINE-5'-DIPHOSPHATE)":133,"Serine/threonine-protein kinase PAK 1":133,"Streptomyces rubiginosus":133,"TRANSCRIPTION, MRNA, MULTIPROTEIN COMPLEX, MOLECULAR MACHINE, DNA, TRANSCRIPTION,TRANSFERASE-DNA-RNA HYBRID COMPLEX":133,"TRANSFERASE/TRANSCRIPTION":133,"Talin-1":133,"Tetracycline repressor protein class D":133,"Tricorn protease":133,"U6 snRNA-associated Sm-like protein LSm5":133,"UBIQUINONE-8":133,"W3110":133,"[acyl-carrier-protein] S-acetyltransferase activity":133,"acyl-CoA hydrolase activity":133,"cAMP metabolic process":133,"cellular response to nitrogen levels":133,"choline binding":133,"chromosome organization":133,"enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity":133,"glutamine binding":133,"histone H3-R2 methylation":133,"kinase, TRANSFERASE-TRANSFERASE INHIBITOR complex":133,"low-density lipoprotein particle receptor catabolic process":133,"muscle myosin complex":133,"myosin filament assembly":133,"negative regulation of exocytosis":133,"negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage":133,"oxidized purine DNA binding":133,"phospholipase C activity":133,"positive regulation of respiratory burst":133,"posttranslational protein targeting to endoplasmic reticulum membrane":133,"protease domain":133,"regulation of cellular respiration":133,"response to jasmonic acid":133,"thymidylate kinase activity":133,"-!- One of several enzymes that catalyze the first step in fatty acids beta-oxidation. -!- The enzyme catalyzes the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. -!- The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. -!- The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA. -!- The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA. -!- Cf. EC 1.3.8.7, EC 1.3.8.8 and EC 1.3.8.9. -!- Formerly EC 1.3.2.1 and EC 1.3.99.2.":132,"-!- Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 on phospholipids, can act as acceptor, but more slowly than H(2)O(2) (cf. EC 1.11.1.12).":132,"-!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1.":132,"-!- This heme-thiolate (P450) enzyme acts on a range of steroids with a 14-alpha-methyl group, such as obtusifoliol and lanosterol. -!- The enzyme catalyzes two successive hydroxylations of the 14-alpha- methyl group, followed by elimination as formate, leaving a 14(15) double bond.":132,"2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O.":132,"2,3-diphosphoglycerate dependent phosphoglycerate mutase. Cofactor dependent phosphoglycerate mutase. PGAM. Phosphoglycerate phosphomutase. Phosphoglyceromutase.":132,"40S ribosomal protein S0-A":132,"40S ribosomal protein S14-A":132,"40S ribosomal protein S9-A":132,"5'-D(*TP*AP*TP*AP*AP*TP*GP*GP*GP*AP*GP*CP*TP*GP*TP*CP*AP*CP*GP*GP*AP*TP*GP*CP*AP*GP*G)-3'":132,"A 14-alpha-methylsteroid + 3 O(2) + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP(+) + 4 H(2)O.":132,"A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.":132,"ANTIFREEZE PROTEIN":132,"ATCC 14579":132,"ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3":132,"Acetobacter pasteurianus":132,"Alicyclobacillus acidocaldarius subsp. acidocaldarius":132,"BAG family molecular chaperone regulator 1":132,"Breast cancer type 1 susceptibility protein":132,"Butanoyl-CoA dehydrogenase. Butyryl dehydrogenase. Short-chain acyl CoA dehydrogenase. Unsaturated acyl-CoA reductase.":132,"CATALYTIC DOMAIN, RESIDUES 32-574":132,"Cystathionine beta-synthase":132,"Cytochrome P450 51. Lanosterol 14-alpha-demethylase. Lanosterol 14-demethylase. Obtusufoliol 14-demethylase.":132,"D-alpha-ornithine 5,4-aminomutase. D-ornithine aminomutase.":132,"D-ornithine 4,5-aminomutase.":132,"D-ornithine = (2R,4S)-2,4-diaminopentanoate.":132,"DNA replication factor C complex":132,"DNA replication, synthesis of RNA primer":132,"Desulfovibrio desulfuricans":132,"Enterotoxin type C-3":132,"Envelope glycoprotein B":132,"GUANOSINE-5',3'-TETRAPHOSPHATE":132,"Geobacillus thermodenitrificans NG80-2":132,"Glutathione peroxidase.":132,"HM-1:IMSS":132,"Hemolysin":132,"LYASE(OXO-ACID)":132,"NAD-dependent protein deacetylase sirtuin-3, mitochondrial":132,"O-GLCNACASE BT_4395":132,"P51 RT":132,"Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).":132,"Protein biosynthesis, ribosome, RNA, EF-G, elongation, factor, GTP, GDPCP, viomycin, tRNA, tranlocation, exit, peptidyl, 50S, 70S, 23S, ribosomal subunit":132,"Protein biosynthesis, ribosome, RNA, tRNA, transfer, exit, peptidyl, 50S, 70S, 23S, ribosomal subunit, streptogramin, antibiotic":132,"Ribonuclease HI":132,"SUGAR (XYLOPYRANOSE)":132,"SWI/SNF complex":132,"Short-chain acyl-CoA dehydrogenase.":132,"Sterol 14-alpha-demethylase.":132,"Syntaxin-1A":132,"Ubiquitin-conjugating enzyme E2 N":132,"Yersinia pseudotuberculosis":132,"chylomicron remnant clearance":132,"clcA, eriC":132,"contractile vacuole organization":132,"creatine biosynthetic process":132,"cybC":132,"diaminopimelate biosynthetic process":132,"inositol metabolic process":132,"lactate biosynthetic process":132,"nanB, SP_1687":132,"negative regulation by symbiont of host protein levels":132,"negative regulation of toll-like receptor 7 signaling pathway":132,"negative regulation of wound healing":132,"positive regulation of histone H4-K16 acetylation":132,"positive regulation of histone H4-K20 methylation":132,"positive regulation of hormone biosynthetic process":132,"positive regulation of synaptic transmission, glutamatergic":132,"protein histidine kinase activity":132,"response to corticosterone":132,"ribosome structure, protein-RNA complex, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, Methylation, Antibiotic resistance, Repressor, Transcription, Transcription regulation, Transcription termination, Translation regulation, tRNA-binding, Phosphoprotein, RIBOSOME":132,"rpoD, TTHA0532":132,"segment polarity determination":132,"serine protease, short hydrogen bond, inhibition mechanism, shift of pKa, trypsin, thrombin, urokinase, factor Xa, hydrolase":132,"viral budding via host ESCRT complex":132,"-!- Has no activating compound but is specific for its substrate. -!- A mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. -!- Phosphorylation inactivates EC 1.2.4.1. -!- Formerly EC 2.7.1.99.":131,"3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL":131,"40S ribosomal protein S17-A":131,"40S ribosomal protein S19-A":131,"40S ribosomal protein S22-A":131,"40S ribosomal protein S25-A":131,"40S ribosomal protein S28-A":131,"40S ribosomal protein S29-A":131,"ADENOSINE-5'-PHOSPHOSULFATE":131,"ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.":131,"Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.":131,"BL21 (DE3)":131,"Beta-N-acetylhexosaminidase":131,"CIRCADIAN CLOCK PROTEIN":131,"Cys-loop receptor family, MEMBRANE PROTEIN, TRANSPORT PROTEIN":131,"Cytosol aminopeptidase":131,"DNA (26-MER)":131,"DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2":131,"Endodeoxyribonucleases producing other than 5'-phosphomonoesters.":131,"FRAGMENT OF MESSENGER RNA":131,"HYGROMYCIN B":131,"Halobacterium salinarum":131,"Heavy Chain":131,"Human immunodeficiency virus type 1 group M subtype B":131,"LEGIONELLA PNEUMOPHILA":131,"Low affinity immunoglobulin epsilon Fc receptor":131,"MB4":131,"MENAQUINONE 8":131,"MIF, GLIF, MMIF":131,"PA":131,"PCC7942":131,"PDH kinase. PDHK. PDK. Pyruvate dehydrogenase kinase. Pyruvate dehydrogenase kinase (phosphorylating).":131,"PLK1, PLK":131,"Phenylalanine--tRNA ligase alpha subunit":131,"RHINOVIRUS COAT PROTEIN, Icosahedral virus, Virus":131,"RNA recognition motif":131,"SOLUTE-BINDING PROTEIN":131,"Sensor protein":131,"Serine O-acetyltransferase.":131,"Signal recognition particle protein":131,"Treponema pallidum subsp. pallidum str. Nichols":131,"U6 snRNA-associated Sm-like protein LSm6":131,"U6 snRNA-associated Sm-like protein LSm7":131,"[Pyruvate dehydrogenase (acetyl-transferring)] kinase.":131,"androsterone dehydrogenase activity":131,"bleb assembly":131,"cell trailing edge":131,"dendrite self-avoidance":131,"dense fibrillar component":131,"detection of mechanical stimulus involved in sensory perception of touch":131,"detection of molecule of bacterial origin":131,"histone demethylase activity (H3-trimethyl-K4 specific)":131,"histone deubiquitination":131,"ksi":131,"lactate dehydrogenase activity":131,"negative regulation of fat cell differentiation":131,"nucleic acid phosphodiester bond hydrolysis":131,"nucleoside-triphosphate diphosphatase activity":131,"phagocytic cup base":131,"phenylpropanoid biosynthetic process":131,"positive regulation of interleukin-2 secretion":131,"positive regulation of protein localization to cell cortex":131,"post-embryonic animal organ development":131,"protein anchor":131,"pyruvate dehydrogenase (acetyl-transferring) kinase activity":131,"response to redox state":131,"scavenger receptor binding":131,"surfactant homeostasis":131,"tRNA aminoacylation":131,"(R)-citrate synthase. Citrate oxaloacetate-lyase ((pro-3S)-CH(2)COO->acetyl-CoA).":130,"-!- Cf. EC 5.4.3.11.":130,"-!- Formerly EC 1.18.96.1.":130,"-!- The stereospecificity of this enzyme is opposite to that of EC 2.3.3.3, which is found in some anaerobes. -!- Formerly EC 4.1.3.7. -!- Citrate synthase for which the stereospecificity with respect to C(2) of oxaloacetate has not been established are included in EC 2.3.3.16.":130,"30S ribosomal subunit, Ribosome, Streptomycin, RNA structure, Thermus thermophilus, Antibiotic resistance, Decoding":130,"5'-R(*UP*UP*CP*AP*AP*AP)-3'":130,"6-phosphofructokinase activity":130,"6-phosphogluconate dehydrogenase, decarboxylating":130,"60S RIBOSOMAL PROTEIN L11":130,"60S RIBOSOMAL PROTEIN L13A":130,"60S RIBOSOMAL PROTEIN L21":130,"60S RIBOSOMAL PROTEIN L31":130,"60S RIBOSOMAL PROTEIN L7":130,"A-SITE MESSENGER RNA FRAGMENT":130,"ALB, GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341":130,"ATCC 17699 / H16 / DSM 428 / Stanier 337":130,"ATCC 27405":130,"Alpha-glucosidase":130,"Brucella suis 1330":130,"CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S":130,"Cell Adhesion":130,"Citrate (Si)-synthase.":130,"Cyclin-T1":130,"DNA POLYMERASE":130,"DNA topoisomerase 4 subunit B":130,"Desulfoferrodoxin. Neelaredoxin.":130,"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex":130,"EGD-E":130,"Escherichia coli DH1":130,"Fumarate reductase subunit C":130,"Fumarate reductase subunit D":130,"Golgi to plasma membrane transport":130,"H-2 class I histocompatibility antigen, L-D alpha chain":130,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)":130,"Hexapeptide repeat proteins":130,"IGHE":130,"L-phenylalanine = L-beta-phenylalanine.":130,"MAPKAPK2":130,"Mayinga-76":130,"Methyl-coenzyme M reductase I subunit beta":130,"Myosin-2 heavy chain":130,"NL4-3":130,"P1-like viruses":130,"PYROCOCCUS HORIKOSHII":130,"Phenylalanine aminomutase (L-beta-phenylalanine forming)":130,"Phenylalanine aminomutase (L-beta-phenylalanine forming).":130,"Polyribonucleotide nucleotidyltransferase":130,"Rac guanyl-nucleotide exchange factor activity":130,"Reduced rubredoxin + superoxide + 2 H(+) = oxidized rubredoxin + H(2)O(2).":130,"Superoxide reductase.":130,"TRANSCRIPTION, TRANSFERASE/DNA":130,"Thermosynechococcus elongatus":130,"beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity":130,"cAMP-dependent protein kinase, alpha-catalytic subunit":130,"ectoderm development":130,"glnA, BSU17460":130,"interleukin-8 secretion":130,"intramolecular transferase activity, transferring amino groups":130,"lamellar body":130,"mRNA stabilization":130,"malate metabolic process":130,"negative regulation of T cell apoptotic process":130,"negative regulation of cell adhesion mediated by integrin":130,"negative regulation of excitatory postsynaptic potential":130,"paclitaxel biosynthetic process":130,"phosphoribosylglycinamide formyltransferase activity":130,"pigs,swine,wild boar":130,"positive regulation of extrinsic apoptotic signaling pathway in absence of ligand":130,"positive regulation of helicase activity":130,"positive regulation of lipoprotein lipase activity":130,"suppression by virus of host cytokine production":130,"vitamin D metabolic process":130,"(1) ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). (2) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).":129,"-!- Involved, together with EC 1.2.7.4 in the synthesis of acetyl-CoA from CO(2) and H(2).":129,"-!- Oxidizes ascorbate and low molecular weight aromatic substrates. -!- The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 or undergoes non-enzymatic disproportionation to ascorbate and dehydroascorbate.":129,"-!- This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1.":129,"17":129,"2 L-ascorbate + H(2)O(2) + 2 H(+) = L-ascorbate + L-dehydroascorbate + 2 H(2)O.":129,"2-PHOSPHOGLYCERIC ACID":129,"ACETONE":129,"ACS.":129,"ALCOHOL DEHYDROGENASE":129,"AQUIFEX AEOLICUS":129,"Acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl- Co(III) corrinoid Fe-S protein].":129,"Ascorbic acid peroxidase.":129,"Bacillus thuringiensis":129,"Bifunctional purine biosynthesis protein PURH":129,"C-terminal fragment, UNP residues 1114-1162":129,"C-terminal fragment, UNP residues 946-1113":129,"CATALASE-PHENOL OXIDASE":129,"CIRCADIAN CLOCK PROTEIN, TRANSFERASE":129,"CO-methylating acetyl-CoA synthase.":129,"CRISPR-associated endonuclease Cas1":129,"Carboxypeptidase B":129,"Cellular retinoic acid-binding protein 2":129,"Cytochrome c oxidase polypeptide 2A":129,"DNA ligation involved in DNA repair":129,"DNA polymerase, TRANSFERASE, LYASE-DNA complex":129,"ENTEROTOXIN":129,"F-actin-capping protein subunit beta isoforms 1 and 2":129,"HLA-DQB1":129,"Hepatitis C virus subtype 1b":129,"IMP cyclohydrolase activity":129,"Infectious bursal disease virus":129,"Integrin alpha-V":129,"L-ascorbate peroxidase.":129,"MALTOSE":129,"Microtubule-associated protein RP/EB family member 3":129,"Mycoplasma pneumoniae M129":129,"Nitrile hydratase alpha subunit":129,"Outer membrane protein F":129,"Plasminogen":129,"Proteasome activator protein PA26":129,"Rotavirus A":129,"Serine translase. SerRS. Seryl-transfer ribonucleate synthetase. Seryl-transfer ribonucleic acid synthetase. Seryl-transfer RNA synthetase. Seryl-tRNA synthetase.":129,"Serine--tRNA ligase.":129,"Shikimate dehydrogenase":129,"TERTIARY-BUTYL ALCOHOL":129,"VIRGINIAMYCIN M1":129,"arrestin family protein binding":129,"brain morphogenesis":129,"cartilage development":129,"cellular response to nicotine":129,"negative regulation of cell proliferation involved in contact inhibition":129,"negative regulation of neuron differentiation":129,"negative regulation of synaptic transmission":129,"orotate phosphoribosyltransferase activity":129,"phosphoribosylaminoimidazolecarboxamide formyltransferase activity":129,"regulation of bile acid biosynthetic process":129,"siderophore biosynthetic process from catechol":129,"triglyceride homeostasis":129,"vesicle docking involved in exocytosis":129,"-!- Favors pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10). -!- Formerly EC 4.2.99.3.":128,"-!- The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. -!- Highly specific for NADP(+). -!- Cf. EC 1.1.1.343.":128,"-!- Thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. -!- Inhibited by 5-methyltetrahydrofolate pentaglutamate. -!- Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.8.3.":128,"2-aminoadipate aminotransferase.":128,"2-aminoadipate transaminase.":128,"6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH.":128,"6-phosphogluconic carboxylase. 6-phosphogluconic dehydrogenase. 6PGD. Phosphogluconic acid dehydrogenase.":128,"ATP-dependent molecular chaperone HSP82":128,"ATPase regulator activity":128,"Alpha-1,4-D-endopolygalacturonic acid lyase. Endo-alpha-1,4-polygalacturonic acid lyase. Endogalacturonate transeliminase. Endopectin methyltranseliminase. Pectate transeliminase. Pectic acid lyase. Pectic acid transeliminase. Pectic lyase. Pectin trans-eliminase. PGA lyase. Polygalacturonate lyase. Polygalacturonic acid lyase. Polygalacturonic acid trans-eliminase. Polygalacturonic transeliminase. PPase-N.":128,"Alpha-xylosidase":128,"Anabaena variabilis":128,"Clostridium sticklandii":128,"Core-binding factor subunit beta":128,"Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.":128,"Eukaryotic translation initiation factor 4E":128,"Friedlin":128,"GLUTATHIONE S-TRANSFERASE CLASS-MU 26 KDA ISOZYME, DYNEIN HEAVY CHAIN CYTOPLASMIC":128,"Glycine N-methyltransferase":128,"Glycine N-methyltransferase.":128,"Glycine methyltransferase.":128,"Guanylate kinase":128,"HEAVY CHAIN (VH) OF FV-FRAGMENT":128,"HIV-1 reverse transcriptase, p51 subunit":128}},"facet_dates":{},"facet_ranges":{}}})