Function and Biology Details
Reaction catalysed:
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Aspartate/ornithine carbamoyltransferase
- Aspartate transcarbamylase regulatory subunit
- Aspartate/ornithine carbamoyltransferase superfamily
- Aspartate carbamoyltransferase
- Aspartate carbamoyltransferase regulatory subunit, C-terminal
- Aspartate carbamoyltransferase regulatory subunit, C-terminal domain superfamily
- Aspartate carbamoyltransferase regulatory subunit, N-terminal
- Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily
2 more domains
Structure analysis Details
Assembly composition:
hetero dodecamer (preferred)
Assembly name:
Aspartate carbamoyltransferase complex (preferred)
PDBe Complex ID:
PDB-CPX-141554 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate carbamoyltransferase catalytic subunit
Molecule details ›
Chains: A, C
Length: 310 amino acids
Theoretical weight: 34.34 KDa
Source organism: Escherichia coli K-12
UniProt:
Sequence domains:
Length: 310 amino acids
Theoretical weight: 34.34 KDa
Source organism: Escherichia coli K-12
UniProt:
- Canonical:
P0A786 (Residues: 2-311; Coverage: 100%)
Sequence domains:
- Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain
- Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain
Aspartate carbamoyltransferase regulatory chain
Molecule details ›
Chains: B, D
Length: 153 amino acids
Theoretical weight: 17.14 KDa
Source organism: Escherichia coli K-12
UniProt:
Sequence domains:
Length: 153 amino acids
Theoretical weight: 17.14 KDa
Source organism: Escherichia coli K-12
UniProt:
- Canonical: P0A7F3 (Residues: 1-153; Coverage: 100%)
Sequence domains:
- Aspartate carbamoyltransferase regulatory chain, allosteric domain
- Aspartate carbamoyltransferase regulatory chain, metal binding domain
