|PROSITE documentation PDOC00393
Fumarate reductase / succinate dehydrogenase FAD-binding site
In bacteria two distinct, membrane-bound, enzyme complexes are responsible for
the interconversion of fumarate and succinate (EC 18.104.22.168): 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 22.214.171.124)
is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulfur
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.
November 1995 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|FRD_SDH_FAD_BINDING, PS00504; Fumarate reductase / succinate dehydrogenase FAD-binding site (PATTERN)
H is the FAD binding site
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1E7P 1KF6 1KFY 1L0V ... [ALL]
||Blaut M., Whittaker K., Valdovinos A., Ackrell B.A., Gunsalus R.P., Cecchini G.
||Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin.
||J. Biol. Chem. 264:13599-13604(1989).
||Birch-Machin M.A., Farnsworth L., Ackrell B.A., Cochran B., Jackson S., Bindoff L.A., Aitken A., Diamond A.G., Turnbull D.M.
||J. Biol. Chem. 267:11553-11558(1992).
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