Carbamoyl-phosphate synthase L chain, ATP binding domain

Definition

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 PMID: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. See [pfam:PF00988]. The small chain has a GATase domain in the carboxyl terminus. See [pfam:PF00117]. The ATP binding domain (this one) has an ATP-grasp fold.

7 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (7 proteins: gene, accession, name)

• ACACA
• ACACB
• CAD
• CPS1
• MCCC1
• PC
• PCCA