Function and Biology Details
Reaction catalysed:
Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
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
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Trimethylamine-N-oxide reductase (preferred)
PDBe Complex ID:
PDB-CPX-155208 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trimethylamine-N-oxide reductase
Molecule details ›
Chain: A
Length: 813 amino acids
Theoretical weight: 90.33 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli DH5[alpha]
UniProt:
Sequence domains:
Length: 813 amino acids
Theoretical weight: 90.33 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli DH5[alpha]
UniProt:
- Canonical:
P44798 (Residues: 41-825; Coverage: 100%)
Sequence domains:
