|PROSITE documentation PDOC00393|
In bacteria two distinct, membrane-bound, enzyme complexes are responsible for the interconversion of fumarate and succinate (EC 220.127.116.11): 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 18.104.22.168) 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 . The sequence around that histidine is well conserved in Frd and Sdh from various bacterial and eukaryotic species  and can be used as a signature pattern.Last update:
November 1995 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Blaut M. Whittaker K. Valdovinos A. Ackrell B.A. Gunsalus R.P. Cecchini G.|
|Title||Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin.|
|Source||J. Biol. Chem. 264:13599-13604(1989).|
|2||Authors||Birch-Machin M.A. Farnsworth L. Ackrell B.A. Cochran B. Jackson S. Bindoff L.A. Aitken A. Diamond A.G. Turnbull D.M.|
|Source||J. Biol. Chem. 267:11553-11558(1992).|