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CATH Superfamily 3.30.470.20

ATP-grasp fold, B domain

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:

"
ATP-grasp fold, B domain
".

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 31345: Carbamoyl-phosphate synthase large chain

There are 7 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
Carbamoyl-phosphate synthase (glutamine-hydrolyzing). [EC: 6.3.5.5]
2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
  • 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.
 1079 A0A015QIK0 A0A015RYU7 A0A015S004 A0A015S3M6 A0A015S8T5 A0A015SHU3 A0A015SR96 A0A015SUP4 A0A015TQG1 A0A015V9E0
(1069 more...)
Aspartate carbamoyltransferase. [EC: 2.1.3.2]
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
    		 35 A0A060T6W0 A0A074T1D8 A0A0B7F5W7 A0A0E3X9Y8 A0A0F8B1B1 A0A0L1HL74 A0A0P4U188 A0A1N6LWW5 A2QRW1 B2RQC6
    (25 more...)
    Carbamoyl-phosphate synthase (ammonia). [EC: 6.3.4.16]
    2 ATP + NH(3) + HCO(3)(-) = 2 ADP + phosphate + carbamoyl phosphate.
    • The enzyme catalyzes the first committed step in the urea cycle.
    • The reaction proceeds via three separate chemical reactions: phosphorylation of hydrogencarbonate to carboxyphosphate; a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate; and the phosphorylation of carbamate forming carbamoyl phosphate.
    • Two moles of ATP are utilized for the synthesis of one molecule of carbamyl phosphate, making the reaction essentially irreversible.
    • The enzyme requires the allosteric activator N-acetyl-L-glutamate.
    • Cf. EC 6.3.5.5.
    • Formerly EC 2.7.2.5.
    		 33 A0A024R454 A0A060RWW6 A0A060THU6 A0A061IFQ2 A0A084G227 A0A084GAP8 A0A086JVB6 A0A086KAJ3 A0A086L898 A0A086Q5S3
    (23 more...)
    Dihydroorotase. [EC: 3.5.2.3]
    (S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.
      		 11 B2RQC6 B7PNL6 E0V8W4 M2XXT9 P05990 P08955 P20054 P27708 Q18990 Q91437
      (1 more...)
      Beta-galactosidase. [EC: 3.2.1.23]
      Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D- galactosides.
      • 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).
      		 2 A0A194PFG8 G6CPP0
      Argininosuccinate synthase. [EC: 6.3.4.5]
      ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate.
        		 1 A0A088RLJ3
        Urea carboxylase. [EC: 6.3.4.6]
        ATP + urea + HCO(3)(-) = ADP + phosphate + urea-1-carboxylate.
        • The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 3.5.1.54, thus bringing about the hydrolysis of urea to CO(2) and NH(3).
        • The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates.
        • Formerly EC 3.5.1.45.
        		 1 T1BZD9
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