CPSase_sm_chain

Carbamoyl-phosphate synthase small chain, CPSase domain
CPSase_sm_chain
SMART accession number:SM01097
Description: The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines (PUBMED:1972379). The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Interpro abstract (IPR002474):

This entry represents the N-terminal domain of the small subunit of carbamoyl phosphate synthase. Structurally, it forms a 3-layer beta/beta/alpha fold of a type that is thought to be mobile in most proteins that carry it [(PUBMED:10587438),(PUBMED:11729189)].

Family alignment:
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There are 8434 CPSase_sm_chain domains in 8430 proteins in SMART's nrdb database.

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