Function and Biology Details
Reaction catalysed:
Naphthalene + NADH + O(2) = (1R,2S)-1,2-dihydronaphthalene-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:
Naphthalene 1,2-dioxygenase system, oxygenase (preferred)
PDBe Complex ID:
PDB-CPX-140970 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Naphthalene 1,2-dioxygenase system, large oxygenase component
Molecule details ›
Chain: A
Length: 449 amino acids
Theoretical weight: 49.62 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 449 amino acids
Theoretical weight: 49.62 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A111 (Residues: 1-449; Coverage: 100%)
Sequence domains:
Structure domains:
Naphthalene 1,2-dioxygenase system, small oxygenase component
Molecule details ›
Chain: B
Length: 194 amino acids
Theoretical weight: 22.97 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
Sequence domains: Ring hydroxylating beta subunit
Structure domains: Nuclear Transport Factor 2; Chain: A,
Length: 194 amino acids
Theoretical weight: 22.97 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
- Canonical: P0A113 (Residues: 1-194; Coverage: 100%)
Sequence domains: Ring hydroxylating beta subunit
Structure domains: Nuclear Transport Factor 2; Chain: A,
