Function and Biology Details
Reaction catalysed:
(1a) dibenzothiophene + FMNH(2) + O(2) = dibenzothiophene-5-oxide + FMN + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Acyl-CoA dehydrogenase, C-terminal domain
- Acyl-CoA dehydrogenase-like, C-terminal
- Acyl-CoA oxidase/dehydrogenase, middle domain
- Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
- Acyl-CoA dehydrogenase/oxidase, N-terminal
- Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
- Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
- Chaperonin-like RbcX superfamily
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Dibenzothiophene monooxygenase (preferred)
PDBe Complex ID:
PDB-CPX-180499 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dibenzothiophene monooxygenase
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 437 amino acids
Theoretical weight: 47.25 KDa
Source organism: Rhodococcus erythropolis XP
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 437 amino acids
Theoretical weight: 47.25 KDa
Source organism: Rhodococcus erythropolis XP
Expression system: Escherichia coli
UniProt:
- Canonical:
Q6WNP1 (Residues: 1-417; Coverage: 100%)
Sequence domains:
- Acyl-CoA dehydrogenase, N-terminal domain
- Acyl-CoA dehydrogenase, middle domain
- Acyl-CoA dehydrogenase, C-terminal domain
