Function and Biology Details
Reaction catalysed:
Vanillyl alcohol + O(2) = vanillin + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Vanillyl-alcohol oxidase, C-terminal subdomain 2
- FAD-binding oxidoreductase/transferase, type 4, C-terminal
- FAD-linked oxidase-like, C-terminal
- Cytokinin dehydrogenase, C-terminal domain superfamily
- FAD-binding, type PCMH, subdomain 2
- FAD linked oxidase, N-terminal
- FAD-binding domain, PCMH-type
- FAD-binding, type PCMH-like superfamily
1 more domain
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
FAD-binding PCMH-type domain-containing protein (preferred)
PDBe Complex ID:
PDB-CPX-171137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-binding PCMH-type domain-containing protein
Molecule details ›
Chains: A, B
Length: 526 amino acids
Theoretical weight: 58.74 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 526 amino acids
Theoretical weight: 58.74 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Escherichia coli
UniProt:
- Canonical:
Q0SBK1 (Residues: 1-526; Coverage: 100%)
Sequence domains:
Structure domains:
