PIG:ETFD

Species (Taxon ID)	Sus scrofa (Pig). (9823)
Gene Name(s)	ETFDH
Protein Name(s)	Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial ETF-QO ETF-ubiquinone oxidoreductase Electron-transferring-flavoprotein dehydrogenase ETF dehydrogenase
External Links
UniProt	P55931
EMBL	EW134518
PDB	2GMH 2GMJ
PDBsum	2GMH 2GMJ
STRING	9823.ENSSSCP00000009469
PaxDb	P55931
eggNOG	COG0644
HOGENOM	HOG000259450
HOVERGEN	HBG005615
InParanoid	P55931
EvolutionaryTrace	P55931
Proteomes	UP000008227
GO	GO:0016020 GO:0005743 GO:0005739 GO:0051539 GO:0009055 GO:0004174 GO:0050660 GO:0051536 GO:0046872 GO:0016491 GO:0043783 GO:0048039 GO:0022900 GO:0006979
InterPro	IPR017896 IPR007859
Pfam	PF05187
PROSITE	PS51379

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0051539	4 iron, 4 sulfur cluster binding	PMID:4052375^[1]	ECO:0000314			F	Methods has references for methods used to determine Fe and S content of the purified protein.	complete
	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	PMID:4052375^[1]	ECO:0000314			F	Purified protein assayed for activity as described in Methods section.	complete
	GO:0050660	FAD binding	PMID:4052375^[1]	ECO:0000314			F	Methods section gives reference for the method used to assay FAD in the purified protein.	complete
enables	GO:0051539	4 iron, 4 sulfur cluster binding	PMID:18037314^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051536	iron-sulfur cluster binding	PMID:17050691^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051536	iron-sulfur cluster binding	PMID:4052375^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0050660	flavin adenine dinucleotide binding	PMID:17050691^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0048039	ubiquinone binding	PMID:17050691^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043783	oxidoreductase activity, oxidizing metal ions with flavin as acceptor	PMID:4052375^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0022900	electron transport chain	PMID:1332770^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	PMID:10423253^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:17050691^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0009055	electron transfer activity	PMID:1332770^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q921G7	P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:1991113^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:4052375^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:1332770^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:10423253^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	PMID:9334218^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051539	4 iron, 4 sulfur cluster binding	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000835262 UniProtKB:P55931 UniProtKB:Q16134	F	Seeded From UniProt	complete
enables	GO:0048039	ubiquinone binding	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000835262 UniProtKB:P55931 UniProtKB:Q16134	F	Seeded From UniProt	complete
enables	GO:0043783	oxidoreductase activity, oxidizing metal ions with flavin as acceptor	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000835262 UniProtKB:P55931	F	Seeded From UniProt	complete
part_of	GO:0031305	integral component of mitochondrial inner membrane	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000065332 UniProtKB:Q16134	C	Seeded From UniProt	complete
involved_in	GO:0022904	respiratory electron transport chain	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000835262 ZFIN:ZDB-GENE-040912-168	P	Seeded From UniProt	complete
enables	GO:0009055	electron transfer activity	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000835262 RGD:735052 UniProtKB:P55931 UniProtKB:Q16134	F	Seeded From UniProt	complete
enables	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0033465 PANTHER:PTN000835262 UniProtKB:P55931 UniProtKB:Q16134	F	Seeded From UniProt	complete
enables	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040156	F	Seeded From UniProt	complete
involved_in	GO:0022900	electron transport chain	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040156	P	Seeded From UniProt	complete
enables	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.5.5.1	F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0249 UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
enables	GO:0051536	iron-sulfur cluster binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0411	F	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
enables	GO:0051539	4 iron, 4 sulfur cluster binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0004	F	Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0999 UniProtKB-SubCell:SL-0168	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Beckmann, JD & Frerman, FE (1985) Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties. Biochemistry 24 3913-21 PubMed GONUTS page
↑ Fielding, AJ et al. (2008) Electron spin relaxation enhancement measurements of interspin distances in human, porcine, and Rhodobacter electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO). J. Magn. Reson. 190 222-32 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Zhang, J et al. (2006) Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Proc. Natl. Acad. Sci. U.S.A. 103 16212-7 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Paulsen, KE et al. (1992) Redox properties of electron-transfer flavoprotein ubiquinone oxidoreductase as determined by EPR-spectroelectrochemistry. Biochemistry 31 11755-61 PubMed GONUTS page
↑ ^5.0 ^5.1 Dwyer, TM et al. (1999) The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer. Biochemistry 38 9735-45 PubMed GONUTS page
↑ Watmough, NJ et al. (1991) Tryptophan fluorescence in electron-transfer flavoprotein:ubiquinone oxidoreductase: fluorescence quenching by a brominated pseudosubstrate. Biochemistry 30 1317-23 PubMed GONUTS page
↑ Salazar, D et al. (1997) Expression and characterization of two pathogenic mutations in human electron transfer flavoprotein. J. Biol. Chem. 272 26425-33 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:4052375-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Beckmann, JD & Frerman, FE (1985) Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties. Biochemistry 24 3913-21 PubMed GONUTS page

[PMID:18037314-2] Fielding, AJ et al. (2008) Electron spin relaxation enhancement measurements of interspin distances in human, porcine, and Rhodobacter electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO). J. Magn. Reson. 190 222-32 PubMed GONUTS page

[PMID:17050691-3] 3.0 ^3.1 ^3.2 ^3.3 Zhang, J et al. (2006) Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Proc. Natl. Acad. Sci. U.S.A. 103 16212-7 PubMed GONUTS page

[PMID:1332770-4] 4.0 ^4.1 ^4.2 Paulsen, KE et al. (1992) Redox properties of electron-transfer flavoprotein ubiquinone oxidoreductase as determined by EPR-spectroelectrochemistry. Biochemistry 31 11755-61 PubMed GONUTS page

[PMID:10423253-5] 5.0 ^5.1 Dwyer, TM et al. (1999) The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer. Biochemistry 38 9735-45 PubMed GONUTS page

[PMID:1991113-6] Watmough, NJ et al. (1991) Tryptophan fluorescence in electron-transfer flavoprotein:ubiquinone oxidoreductase: fluorescence quenching by a brominated pseudosubstrate. Biochemistry 30 1317-23 PubMed GONUTS page

[PMID:9334218-7] Salazar, D et al. (1997) Expression and characterization of two pathogenic mutations in human electron transfer flavoprotein. J. Biol. Chem. 272 26425-33 PubMed GONUTS page

[PMID:21873635-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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PIG:ETFD

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