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InterPro: IPR003952 Fumarate reductase/succinate dehydrogenase, FAD-binding site

Protein matches Help

UniProtKB

Matches:

1659 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003952 FRD_SDH_FAD_BS

Secondary

IPR000464

Type

Binding_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00504	FRD_SDH_FAD_BINDING	1659
Signatures in BioMart

InterPro Relationships Help

Found in

IPR003953 Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
IPR005884 Fumarate reductase, flavoprotein subunit
IPR011281 Succinate dehydrogenase, flavoprotein subunit
IPR013027 FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR014006 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

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-sulphur 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-sulphur 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].

Structural links Help

PDB - click here

SCOP: c.3.1.4

CATH: 3.50.50.60

Database links Help

PDBe-motif: PS00504

Enzyme: EC:1.3

PROSITE doc: PDOC00393

Blocks: IPB003952

COMe: PRX000347

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003952

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P31040 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

P47052 Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial

Q09508 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Q8K2B3 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Q94523 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR015939	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
IPR014006	Succinate dehydrogenase/fumarate reductase, flavoprotein subunit
IPR004112	Fumarate reductase/succinate dehydrogenase flavoprotein, C-terminal
IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR011281	Succinate dehydrogenase, flavoprotein subunit
IPR003952	Fumarate reductase/succinate dehydrogenase, FAD-binding site
IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Blaut M, Whittaker K, Valdovinos A, Ackrell BA, Gunsalus RP, Cecchini G. Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin. J. Biol. Chem. 264 13599-604 1989 [PubMed: 2668268] http://intl.jbc.org/cgi/reprint/264/23/13599.pdf
2.	Birch-Machin MA, Farnsworth L, Ackrell BA, Cochran B, Jackson S, Bindoff LA, Aitken A, Diamond AG, Turnbull DM. The sequence of the flavoprotein subunit of bovine heart succinate dehydrogenase. J. Biol. Chem. 267 11553-8 1992 [PubMed: 1375942] http://intl.jbc.org/cgi/reprint/267/16/11553.pdf

Additional Reading Open in usermanual
	Tomasiak TM, Maklashina E, Cecchini G, Iverson TM. A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II. J. Biol. Chem. 283 2008 15460-8 [PubMed: 18385138] http://dx.doi.org/10.1074/jbc.M801372200
	Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mantele W, Simon J, Madej MG. Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase. Proc. Natl. Acad. Sci. U.S.A. 102 2005 18860-5 [PubMed: 16380425] http://dx.doi.org/10.1073/pnas.0509711102
	Madej MG, Nasiri HR, Hilgendorff NS, Schwalbe H, Lancaster CR. Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex. EMBO J. 25 2006 4963-70 [PubMed: 17024183] http://dx.doi.org/10.1038/sj.emboj.7601361
	Maklashina E, Iverson TM, Sher Y, Kotlyar V, Andrell J, Mirza O, Hudson JM, Armstrong FA, Rothery RA, Weiner JH, Cecchini G. Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain. J. Biol. Chem. 281 2006 11357-65 [PubMed: 16484232] http://dx.doi.org/10.1074/jbc.M512544200
	Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science 299 2003 700-4 [PubMed: 12560550] http://dx.doi.org/10.1126/science.1079605

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