CATH Classification

Domain Context

CATH Clusters

Superfamily Dimethylsulfoxide Reductase, domain 3
Functional Family

Enzyme Information

1.7.2.3
Trimethylamine-N-oxide reductase.
based on mapping to UniProt Q52675
Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+).
-!- Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. -!- The reductant is a membrane-bound multiheme cytochrome c. -!- Also reduces dimethyl sulfoxide to dimethyl sulfide.
1.8.5.3
Respiratory dimethylsulfoxide reductase.
based on mapping to UniProt Q52675
Dimethylsulfide + menaquinone + H(2)O = dimethylsulfoxide + menaquinol.
-!- The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor. -!- It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron- sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool. -!- The electrons are passed through DmsB to DmsA and on to DMSO. -!- The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.

UniProtKB Entries (1)

Q52675
DSTOR_RHOCA
Rhodobacter capsulatus
Dimethyl sulfoxide/trimethylamine N-oxide reductase

PDB Structure

PDB 1E61
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Reversible Dissociation of Thiolate Ligands from Molybdenum in an Enzyme of the Dimethyl Sulfoxide Reductase Family
Bray, R.C., Adams, B., Smith, A.T., Bennett, B., Bailey, S.
Biochemistry