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InterPro: IPR003953 Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal

Protein matches Help

UniProtKB

Matches:

7194 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

IPR003953 FAD_bind2_N

Secondary

IPR000464

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00890	FAD_binding_2	7194
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005288 L-aspartate oxidase
IPR005884 Fumarate reductase, flavoprotein subunit
IPR006277 Sarcosine oxidase, alpha subunit, heterotetrameric
IPR009158 Anaerobic glycerol-3-phosphate dehydrogenase, subunit B
IPR010960 Flavocytochrome c
IPR011280 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit, low-GC Gram-positive bacteria
IPR011281 Succinate dehydrogenase, flavoprotein subunit
IPR011803 Adenylylsulphate reductase, alpha subunit
IPR012400 Long-chain fatty alcohol dehydrogenase
IPR014614 Uncharacterised conserved protein UCP036654

Contains

IPR003952 Fumarate reductase/succinate dehydrogenase, FAD-binding site

GO Term annotation Help

Function

GO:0009055 electron carrier activity
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].

This family includes members that bind FAD such as the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.

Structural links Help

PDB - click here

SCOP: c.3.1.4 , d.168.1.1

CATH: 3.50.50.60 , 3.90.700.10

Database links Help

Enzyme: EC:1

PANDIT: PF00890

Blocks: IPB003953

COMe: PRX000344

Pfam Clan: CL0063.21

AC	CL0063.21
ID	NADP_Rossmann
DE	FAD/NAD(P)-binding Rossmann fold Superfamily
PF00044	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
PF00056	IPR001236	Lactate/malate dehydrogenase
PF00070	IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00106	IPR002198	Short-chain dehydrogenase/reductase SDR
PF00107	IPR013149	Alcohol dehydrogenase, zinc-binding
PF00208	IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
PF00479	IPR001282	Glucose-6-phosphate dehydrogenase
PF00670	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
PF00732	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
PF00743	IPR000960	Flavin-containing monooxygenase FMO
PF00890	IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00899	IPR000594	UBA/THIF-type NAD/FAD binding fold
PF00996	IPR018203	GDP dissociation inhibitor
PF01073	IPR002225	3-beta hydroxysteroid dehydrogenase/isomerase
PF01113	IPR000846	Dihydrodipicolinate reductase
PF01118	IPR000534	Semialdehyde dehydrogenase, NAD-binding
PF01134	IPR002218	Glucose-inhibited division protein A-related
PF01210	IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01225	IPR000713	Mur ligase, N-terminal
PF01232	IPR013131	Mannitol dehydrogenase, N-terminal
PF01262	IPR007698	Alanine dehydrogenase/PNT, C-terminal
PF01266	IPR006076	FAD dependent oxidoreductase
PF01370	IPR001509	NAD-dependent epimerase/dehydratase
PF01408	IPR000683	Oxidoreductase, N-terminal
PF01488	IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
PF01494	IPR002938	Monooxygenase, FAD-binding
PF01593	IPR002937	Amine oxidase
PF01946	IPR002922	Thiamine biosynthesis Thi4 protein
PF02153	IPR003099	Prephenate dehydrogenase
PF02254	IPR003148	Regulator of K+ conductance, N-terminal
PF02423	IPR003462	Ornithine cyclodeaminase/mu-crystallin
PF02558	IPR013332	Ketopantoate reductase ApbA/PanE, N-terminal
PF02629	IPR003781	CoA-binding
PF02670	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02719	IPR003869	Polysaccharide biosynthesis protein CapD-like
PF02737	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
PF02826	IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02882	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
PF03435	IPR005097	Saccharopine dehydrogenase
PF03446	IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
PF03447	IPR005106	Aspartate/homoserine dehydrogenase, NAD-binding
PF03486	IPR004792	HI0933-like protein
PF03721	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03807	IPR004455	NADP oxidoreductase, coenzyme F420-dependent
PF03949	IPR012302	Malic enzyme, NAD-binding
PF04321	IPR005913	dTDP-4-dehydrorhamnose reductase
PF04723	IPR006812	Glycine reductase complex selenoprotein A
PF04820	IPR006905	Tryptophan halogenase
PF05368	IPR008030	NmrA-like
PF05834	IPR008671	Lycopene beta/epsilon cyclase
PF06039	IPR006231	Malate:quinone-oxidoreductase
PF07157	IPR009826	DNA circulation, N-terminal
PF07991	IPR013116	Acetohydroxy acid isomeroreductase, catalytic
PF07992	IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07993	IPR013120	Male sterility, NAD-binding
PF07994	IPR002587	Myo-inositol-1-phosphate synthase
PF08491	IPR013698	Squalene epoxidase
PF08659	IPR013968	Polyketide synthase, KR
PF10727	IPR019665	Putative oxidoreductase/dehydrogenase, Rossmann-like domain

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003953

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P21375 Osmotic growth protein 1

P31040 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Q09508 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Q64FW2 All-trans-retinol 13,14-reductase

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
IPR010960	Flavocytochrome c
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
	Mittl PR, Schulz GE. Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Protein Sci. 3 1994 799-809 [PubMed: 8061609] http://www.proteinscience.org/cgi/content/abstract/3/5/799
	Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK. A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. J. Biol. Chem. 281 2006 20589-97 [PubMed: 16699170] http://dx.doi.org/10.1074/jbc.M603077200

InterPro 23.1