Function and Biology Details
Reaction catalysed:
Salicylate + NADH + O(2) = 2,5-dihydroxybenzoate + NAD(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Aromatic-ring-hydroxylating dioxygenase, alpha subunit
- Rieske [2Fe-2S] iron-sulphur domain
- Rieske [2Fe-2S] iron-sulphur domain superfamily
- SnoaL-like domain
- Ring-hydroxylating dioxygenase beta subunit
- NTF2-like domain superfamily
- Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain
- Ring-hydroxylating dioxygenase, large/alpha subunit AhdA1c-like, C-terminal
1 more domain
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Salicylate 5-hydroxylase, oxygenase (preferred)
PDBe Complex ID:
PDB-CPX-520487 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Salicylate 5-hydroxylase, large oxygenase component
Molecule details ›
Chains: A, C, E, G
Length: 442 amino acids
Theoretical weight: 50.95 KDa
Source organism: Ralstonia sp.
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 442 amino acids
Theoretical weight: 50.95 KDa
Source organism: Ralstonia sp.
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O52379 (Residues: 1-423; Coverage: 100%)
Sequence domains:
Salicylate 5-hydroxylase, small oxygenase component
Molecule details ›
Chains: B, D, F, H
Length: 161 amino acids
Theoretical weight: 18.83 KDa
Source organism: Ralstonia sp.
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: SnoaL-like domain
Length: 161 amino acids
Theoretical weight: 18.83 KDa
Source organism: Ralstonia sp.
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: O52380 (Residues: 1-161; Coverage: 100%)
Sequence domains: SnoaL-like domain
