Function and Biology Details
Reaction catalysed:
Biphenyl + NADH + O(2) = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Aromatic-ring-hydroxylating dioxygenase, alpha subunit
- Ring-hydroxylating dioxygenase beta subunit
- Rieske [2Fe-2S] iron-sulphur domain
- Rieske [2Fe-2S] iron-sulphur domain superfamily
- NTF2-like domain superfamily
- Ring-hydroxylating dioxygenase, alpha subunit NdoB-like, C-terminal
- Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain
- Aromatic-ring-hydroxylating dioxygenase, 2Fe-2S-binding site
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Biphenyl 2,3-dioxygenase (preferred)
PDBe Complex ID:
PDB-CPX-176045 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Biphenyl 2,3-dioxygenase subunit alpha
Molecule details ›
Chains: A, C, E
Length: 460 amino acids
Theoretical weight: 51.64 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Rhodococcus erythropolis
UniProt:
Sequence domains:
Structure domains:
Length: 460 amino acids
Theoretical weight: 51.64 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Rhodococcus erythropolis
UniProt:
- Canonical:
Q53122 (Residues: 1-460; Coverage: 100%)
Sequence domains:
Structure domains:
Biphenyl 2,3-dioxygenase subunit beta
Molecule details ›
Chains: B, D, F
Length: 187 amino acids
Theoretical weight: 22.05 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Rhodococcus erythropolis
UniProt:
Sequence domains: Ring hydroxylating beta subunit
Structure domains: Nuclear Transport Factor 2; Chain: A,
Length: 187 amino acids
Theoretical weight: 22.05 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Rhodococcus erythropolis
UniProt:
- Canonical: Q53123 (Residues: 1-187; Coverage: 100%)
Sequence domains: Ring hydroxylating beta subunit
Structure domains: Nuclear Transport Factor 2; Chain: A,
