Function and Biology Details
Reaction catalysed:
3,4-dihydroxyphenylacetate + O(2) = 2-hydroxy-5-carboxymethylmuconate semialdehyde
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
- Glyoxalase/fosfomycin resistance/dioxygenase domain
- Vicinal oxygen chelate (VOC) domain
- 3,4-dihydroxyphenylacetate 2,3-dioxygenase, C-terminal domain superfamily
- Extradiol ring-cleavage dioxygenase, class I /II
- 3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn/Fe-type
Structure domain:
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
VOC domain-containing protein (preferred)
PDBe Complex ID:
PDB-CPX-175006 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
VOC domain-containing protein
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 36.99 KDa
Source organism: Arthrobacter globiformis
Expression system: Escherichia coli
UniProt:
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1
Length: 323 amino acids
Theoretical weight: 36.99 KDa
Source organism: Arthrobacter globiformis
Expression system: Escherichia coli
UniProt:
- Canonical:
Q44048 (Residues: 1-235, 236-322; Coverage: 94%)
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1
