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CATH Superfamily 3.30.1490.20

ATP-grasp fold, A 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, A 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 22291: Carbamoyl-phosphate synthase [ammonia], mitochondr...

There are 1 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 (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.
 6 A0A024R454 P07756 P31327 Q3S2E9 Q8C196 Q91293