PROSITE documentation PDOC00393

Fumarate reductase / succinate dehydrogenase FAD-binding site




Description

In bacteria two distinct, membrane-bound, enzyme complexes are responsible for the interconversion of fumarate and succinate (EC 1.3.99.1): fumarate reductase (Frd) is used in anaerobic growth, and succinate dehydrogenase (Sdh) is used in aerobic growth. Both complexes consist of two main components: a membrane-extrinsic component composed of a FAD-binding flavoprotein and an iron-sulfur protein; and an hydrophobic component composed of a membrane anchor protein and/or a cytochrome B.

In eukaryotes mitochondrial succinate dehydrogenase (ubiquinone) (EC 1.3.5.1) is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulfur protein.

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-terminal section of the protein [1]. The sequence around that histidine is well conserved in Frd and Sdh from various bacterial and eukaryotic species [2] and can be used as a signature pattern.

Last update:

November 1995 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

FRD_SDH_FAD_BINDING, PS00504; Fumarate reductase / succinate dehydrogenase FAD-binding site  (PATTERN)


References

1AuthorsBlaut M., Whittaker K., Valdovinos A., Ackrell B.A., Gunsalus R.P., Cecchini G.
TitleFumarate reductase mutants of Escherichia coli that lack covalently bound flavin.
SourceJ. Biol. Chem. 264:13599-13604(1989).
PubMed ID2668268

2AuthorsBirch-Machin M.A., Farnsworth L., Ackrell B.A., Cochran B., Jackson S., Bindoff L.A., Aitken A., Diamond A.G., Turnbull D.M.
SourceJ. Biol. Chem. 267:11553-11558(1992).



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