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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)
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
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• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00504
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• Scan Swiss-Prot/TrEMBL entries against PS00504
• view ligand binding statistics
Matching PDB structures: 1E7P 1KF6 1KFY 1L0V ... [ALL]

References:

1 AuthorsBlaut 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
2 AuthorsBirch-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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