Protein Domain : IPR005884

Type:  Family Name:  Fumarate reductase, flavoprotein subunit
Description:  In bacteria two distinct, membrane-bound, enzyme complexes are responsible for the interconversion of fumarate and succinate (): fumaratereductase (Frd) is used in anaerobic growth, and succinate dehydrogenase (Sdh) is used in aerobic growth. Both complexes consist of two main components: amembrane-extrinsic component composed of a FAD-binding flavoprotein and an iron-sulphur protein; and an hydrophobic component composed of a membraneanchor protein and/or a cytochrome B.In eukaryotes mitochondrial succinate dehydrogenase (ubiquinone) () is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulphurprotein.The flavoprotein subunit is a protein of about 60 to 70 Kd to which FAD is covalently bound to a histidine residue which is located in the N-terminalsection of the protein []. The sequence around that histidine is well conserved in Frd and Sdh from various bacterial and eukaryotic species [].The terms succinate dehydrogenase and fumarate reductase may be used interchangeably in certain systems. However, a number of species have distinct complexes, with the fumarate reductase active under anaerobic conditions. This model represents the fumarate reductase flavoprotein subunit from several such species in which a distinct succinate dehydrogenase is also found. Short Name:  Fum_red_fp

0 Child Features

2 Contains

DB identifier Type Name
IPR003953 Domain FAD-dependent oxidoreductase 2, FAD binding domain
IPR003952 Binding_site Fumarate reductase/succinate dehydrogenase, FAD-binding site

1 Cross References

Identifier
TIGR01176

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0016491 IPR005884
GO:0009061 IPR005884
GO:0055114 IPR005884

3 Ontology Annotations

GO Term Gene Name
GO:0016491 IPR005884
GO:0009061 IPR005884
GO:0055114 IPR005884

1 Parent Features

DB identifier Type Name
IPR014006 Family Succinate dehydrogenase/fumarate reductase, flavoprotein subunit

0 Proteins

2 Publications

First Author Title Year Journal Volume Pages PubMed ID
            2668268
            1375942