Function and Biology Details
Reaction catalysed:
(1a) 4-methylphenol + 2 oxidized azurin + H(2)O = 4-hydroxybenzyl alcohol + 2 reduced azurin + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Cytochrome c-like domain
- Cytochrome c-like domain superfamily
- 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
3 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
4-cresol dehydrogenase [hydroxylating] (preferred)
PDBe Complex ID:
PDB-CPX-140744 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit
Molecule details ›
Chains: A, B
Length: 520 amino acids
Theoretical weight: 57.87 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 520 amino acids
Theoretical weight: 57.87 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
- Canonical:
P09788 (Residues: 2-521; Coverage: 100%)
Sequence domains:
Structure domains:
4-cresol dehydrogenase [hydroxylating] cytochrome c subunit
Molecule details ›
Chains: C, D
Length: 80 amino acids
Theoretical weight: 8.61 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
Sequence domains: Cytochrome C oxidase, cbb3-type, subunit III
Structure domains: Cytochrome c-like domain
Length: 80 amino acids
Theoretical weight: 8.61 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
- Canonical: P09787 (Residues: 34-113; Coverage: 100%)
Sequence domains: Cytochrome C oxidase, cbb3-type, subunit III
Structure domains: Cytochrome c-like domain
