Function and Biology Details
Reactions catalysed:
(1a) ATP + HCO(3)(-) = ADP + carboxyphosphate
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Carbamoyl-phosphate synthase large subunit, CPSase domain
- Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
- Methylglyoxal synthase-like domain
- Carbamoyl-phosphate synthase, large subunit
- Class I glutamine amidotransferase-like
- Carbamoyl-phosphate synthase, small subunit
- Carbamoyl-phosphate synthase small subunit, N-terminal domain
- Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily
8 more domains
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
Carbamoyl phosphate synthase (preferred)
PDBe Complex ID:
PDB-CPX-133742 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carbamoyl phosphate synthase large chain
Molecule details ›
Chains: B, E, H, K
Length: 1073 amino acids
Theoretical weight: 117.98 KDa
Source organism: Escherichia coli
UniProt:
Sequence domains:
Length: 1073 amino acids
Theoretical weight: 117.98 KDa
Source organism: Escherichia coli
UniProt:
- Canonical:
P00968 (Residues: 1-1073; Coverage: 100%)
Sequence domains:
- Carbamoyl-phosphate synthase L chain, ATP binding domain
- Carbamoyl-phosphate synthetase large chain, oligomerisation domain
- MGS-like domain
Carbamoyl phosphate synthase small chain
Molecule details ›
Chains: C, F, I, L
Length: 382 amino acids
Theoretical weight: 41.48 KDa
Source organism: Escherichia coli
UniProt:
Sequence domains:
Length: 382 amino acids
Theoretical weight: 41.48 KDa
Source organism: Escherichia coli
UniProt:
- Canonical: P0A6F1 (Residues: 1-382; Coverage: 100%)
Sequence domains:
- Carbamoyl-phosphate synthase small chain, CPSase domain
- Glutamine amidotransferase class-I
- Peptidase C26
