{PDOC00393}
{PS00504; FRD_SDH_FAD_BINDING}
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* Fumarate reductase / succinate dehydrogenase FAD-binding site *
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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.

-Consensus pattern: R-[ST]-H-[ST]-x(2)-A-x-G-G
                    [H is the FAD binding site]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 1995 / Pattern and text revised.

[ 1] 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).
     PubMed=2668268
[ 2] 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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