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 1DMS
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution.
Schneider, F., Lowe, J., Huber, R., Schindelin, H., Kisker, C., Knablein, J.
J.Mol.Biol.