Function and Biology Details
Reaction catalysed:
L-carnitine + NAD(P)H + O(2) = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Aromatic-ring-hydroxylating dioxygenase, alpha subunit
- Rieske [2Fe-2S] iron-sulphur domain
- Rieske [2Fe-2S] iron-sulphur domain superfamily
- Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain
- Aromatic-ring-hydroxylating dioxygenase, 2Fe-2S-binding site
- Carnitine monooxygenase oxygenase subunit
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
Carnitine monooxygenase oxygenase subunit (preferred)
PDBe Complex ID:
PDB-CPX-100289 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnitine monooxygenase oxygenase subunit
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 391 amino acids
Theoretical weight: 44.78 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 391 amino acids
Theoretical weight: 44.78 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0A059ZPP5 (Residues: 1-371; Coverage: 100%)
Sequence domains:
