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CATH Superfamily 3.30.200.20

Phosphorylase Kinase; domain 1

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Phosphorylase Kinase; domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 66995: Acyl-CoA dehydrogenase family member 10

There are 12 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
ATP + a protein = ADP + a phosphoprotein.
  • 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.
 166 A0A060RTE5 A0A060RTE5 A0A061IEH6 A0A061IEH6 A0A061IH21 A0A061IH21 A0A062VBS2 A0A062VBS2 A0A074TBV4 A0A074TBV4
(156 more...)
Kanamycin kinase. [EC: 2.7.1.95]
ATP + kanamycin = ADP + kanamycin 3'-phosphate.
  • Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A.
  • An enzyme from Pseudomonas aeruginosa also acts on butirosin.
 24 A0A0K1EF61 A0A0K1EF61 A0A0X8R757 A0A0X8R757 A0A173KZH8 A0A173KZH8 G0ERH1 G0ERH1 G0F0B4 G0F0B4
(14 more...)
Glutaminyl-tRNA synthase (glutamine-hydrolyzing). [EC: 6.3.5.7]
ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
  • In systems lacking discernible EC 6.1.1.18, glutaminyl-tRNA(Gln) is formed by a two-enzyme system.
  • In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln).
  • The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl- tRNA(Glu) is not a substrate for this reaction).
  • Ammonia or asparagine can substitute for the preferred substrate glutamine.
 10 A0A0V0RIQ5 A0A0V0RIQ5 A0A0V0WGP2 A0A0V0WGP2 A0A0V0ZGB9 A0A0V0ZGB9 A0A0V1B8S8 A0A0V1B8S8 A0A0V1LBL6 A0A0V1LBL6
Medium-chain acyl-CoA dehydrogenase. [EC: 1.3.8.7]
A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
  • One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
  • The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C(8) to C(12) compounds.
  • The enzyme from rat does not accept C(16) at all and is most active with C(6)-C(8) compounds.
  • cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9.
  • Formerly EC 1.3.2.2 and EC 1.3.99.3.
 8 A0A173KSP1 A0A173KSP1 A0A173L1F7 A0A173L1F7 U2E6G5 U2E6G5 U2FWT0 U2FWT0
Homoserine kinase. [EC: 2.7.1.39]
ATP + L-homoserine = ADP + O-phospho-L-homoserine.
    		 6 A0A0G3XVD9 A0A0G3XVD9 A0A0N0I8J3 A0A0N0I8J3 A0A1J5Q8G9 A0A1J5Q8G9
    Enoyl-CoA hydratase. [EC: 4.2.1.17]
    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
    • Acts in the reverse direction.
    • With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74).
    		 4 A0A059MKK5 A0A059MKK5 N1M6C5 N1M6C5
    Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9. [EC: 1.3.99.3]
      		2 A9HVQ1 A9HVQ1
      Short-chain acyl-CoA dehydrogenase. [EC: 1.3.8.1]
      A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
      • 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.
      		 2 N1M603 N1M603
      Thiamine phosphate synthase. [EC: 2.5.1.3]
      (1) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy- 4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (2) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4- methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (3) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5- (2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.
      • The enzyme catalyzes the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components.
      • The enzyme is thought to accept the product of EC 2.8.1.10 as its substrate.
      • However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, EC 5.3.99.10 converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase.
      • In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products.
      • In yeast this activity is found in a bifunctional enzyme and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme.
      		 2 A6FNB2 A6FNB2
      Phosphoenolpyruvate carboxykinase (ATP). [EC: 4.1.1.49]
      ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2).
        		 2 A0A075AZW4 A0A075AZW4
        (R)-benzylsuccinyl-CoA dehydrogenase. [EC: 1.3.8.3]
        (R)-2-benzylsuccinyl-CoA + electron-transfer flavoprotein = (E)-2- benzylidenesuccinyl-CoA + reduced electron-transfer flavoprotein.
        • Unlike other acyl-CoA dehydrogenases, this enzyme exhibits high substrate- and enantiomer specificity it is highly specific for (R)- benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA.
        • Forms the third step in the anaerobic toluene metabolic pathway in Thauera aromatica.
        • Ferricenium ion is an effective artificial electron acceptor.
        • Formerly EC 1.3.99.21.
        		 2 A0A0M7HJD5 A0A0M7HJD5
        3-isopropylmalate dehydratase. [EC: 4.2.1.33]
        (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.
        • Forms part of the leucine-biosynthesis pathway.
        • Brings about the interconversion of the two isomers of isopropylmalate.
        		 2 U2WS27 U2WS27
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