Function and Biology Details
Reactions catalysed:
(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Aspartate/ornithine carbamoyltransferase
- Aspartate/ornithine carbamoyltransferase superfamily
- Dihydroorotase, conserved site
- Dihydroorotase
- Metal-dependent hydrolase, composite domain superfamily
- Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain
- Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
- Aspartate carbamoyltransferase
3 more domains
Structure analysis Details
Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130369 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydroorotase
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 50.3 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Amidohydrolase family
Structure domains:
Length: 456 amino acids
Theoretical weight: 50.3 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O66990 (Residues: 1-422; Coverage: 100%)
Sequence domains: Amidohydrolase family
Structure domains:
Aspartate carbamoyltransferase catalytic subunit
Molecule details ›
Chain: B
Length: 322 amino acids
Theoretical weight: 37.14 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 322 amino acids
Theoretical weight: 37.14 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: O66726 (Residues: 1-291; Coverage: 100%)
Sequence domains:
- Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain
- Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain
