CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.40 | Barwin-like endoglucanases |
|
2.40.40.20 |
Domain Context
CATH Clusters
| Superfamily | 2.40.40.20 |
| Functional Family | Biotin sulfoxide reductase 2 |
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 | 3DMR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Molybdenum Active Centre of Dmso Reductase from Rhodobacter Capsulatus: Crystal Structure of the Oxidised Enzyme at 1.82-A Resolution and the Dithionite-Reduced Enzyme at 2.8-A Resolution
J.Biol.Inorg.Chem.
|
