Protein Domain : IPR011888

Type:  Family Name:  Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE
Description:  Many bacterial species are capable of anaerobic growth by using dimethylsulphoxide (DMSO) as the terminal electron acceptor, with DMSO reductase as the terminal elctron transfer enzyme. In Escherichia coliand many other Gram-negative bacteria DMSO reductase is a membrane-bound enzyme composed of three subunits; a catalytic molybdenum-containing subunit (DmsA), an electron transfer subunit containing a [4Fe-4S] cluster (DmsB), and a hydrophobic membrane-spanning anchor subunit which attaches the enzyme to the cytoplasmic membrane (DmsC) [, ]. It is generally thought now that DmsAB faces the periplasm, contradicting previous results suggesting a cytoplasmic location. The N-terminal region of DmsA contains a "twin-arginine" signal sequence, suggesting export to the periplasm occurs via the TAT secretion pathway.This entry represents known and predicted bacterial DmsA polypeptides. Several species contain one or more paralogs of DmsA. In E. coli, the two paralogs of DmsA, YnfE and YnfF, are encoded within the ynfEFGHI operon []. YnfE and YnfF cannot form a functional complex with DmsBC, but YnfFGH can restore growth on DMSO when DmABC is deleted. The function of YnfE is not known and it appears to prevent formation of the YnfFGH complex if present. Short Name:  Anaer_DMSO_reductase

0 Child Features

4 Contains

DB identifier Type Name
IPR006656 Domain Molybdopterin oxidoreductase
IPR006311 Conserved_site Twin-arginine translocation pathway, signal sequence
IPR006657 Domain Molybdopterin dinucleotide-binding domain
IPR006655 Conserved_site Molybdopterin oxidoreductase, prokaryotic, conserved site

1 Cross References

Identifier
TIGR02166

0 Found In

4 GO Annotations

GO Term Gene Name
GO:0009389 IPR011888
GO:0030151 IPR011888
GO:0051539 IPR011888
GO:0055114 IPR011888

4 Ontology Annotations

GO Term Gene Name
GO:0009389 IPR011888
GO:0030151 IPR011888
GO:0051539 IPR011888
GO:0055114 IPR011888

0 Parent Features

0 Proteins

3 Publications

First Author Title Year Journal Volume Pages PubMed ID
            16221580
            1324728
            14522592