Function and Biology Details
Reactions catalysed:
Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+)
Dimethylsulfide + menaquinone + H(2)O = dimethylsulfoxide + menaquinol
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Molybdopterin oxidoreductase, prokaryotic, conserved site
- Molybdopterin dinucleotide-binding domain
- Trimethylamine-N-oxide reductase-like, molybdopterin-binding domain
- Aspartate decarboxylase-like domain superfamily
- Molybdopterin oxidoreductase
- Molybdopterin guanine dinucleotide-containing S/N-oxide reductase
- Molybdopterin oxidoreductase, N-terminal
- Twin-arginine translocation pathway, signal sequence
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176016 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dimethyl sulfoxide/trimethylamine N-oxide reductase
Molecule details ›
Chains: A, C
Length: 823 amino acids
Theoretical weight: 89.53 KDa
Source organism: Rhodobacter capsulatus
UniProt:
Sequence domains:
Length: 823 amino acids
Theoretical weight: 89.53 KDa
Source organism: Rhodobacter capsulatus
UniProt:
- Canonical:
Q52675 (Residues: 1-823; Coverage: 100%)
Sequence domains:
- Molybdopterin oxidoreductase N-terminal domain
- Molybdopterin oxidoreductase
- Molydopterin dinucleotide binding domain
