PIG:ETFD

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Species (Taxon ID)	Sus scrofa (Pig). (taxon: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 Identifier	ETFD_PIG
UniProt Accessions	P55931,
EMBL	EW134518,
PDB	2GMH, 2GMJ,
Pfam	PF05187,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0016021	integral to membrane		IEA: Inferred from Electronic Annotation		C	Source: UniProtKB-KW
	GO:0005743	mitochondrial inner membrane		IEA: Inferred from Electronic Annotation		C	Source: UniProtKB-SubCell
	GO:0051539	4 iron, 4 sulfur cluster binding	PMID:4052375^[1]	IDA: Inferred from Direct Assay		F	Methods has references for methods used to determine Fe and S content of the purified protein.	complete
	GO:0004174	electron-transferring-flavoprotein dehydrog...		IEA: Inferred from Electronic Annotation		F	Source: EC
	GO:0005506	iron ion binding		IEA: Inferred from Electronic Annotation		F	Source: UniProtKB-KW
	GO:0022900	electron transport chain		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
	GO:0006810	transport		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	PMID:4052375^[1]	IDA: Inferred from Direct Assay		F	Purified protein assayed for activity as described in Methods section.	complete
	GO:0050660	FAD binding	PMID:4052375^[1]	IDA: Inferred from Direct Assay		F	Methods section gives reference for the method used to assay FAD in the purified protein.	complete
	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR007859	F
	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:1.5.5.1	F
	GO:0004174	electron-transferring-flavoprotein dehydrogenase activity	PMID:9334218^[2]	IDA: Inferred from Direct Assay		F
	GO:0005739	mitochondrion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0496	C
	GO:0005743	mitochondrial inner membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0999	C
	GO:0005743	mitochondrial inner membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0168	C
	GO:0006810	transport	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0813	P
	GO:0006979	response to oxidative stress	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q921G7	P
	GO:0009055	electron carrier activity	PMID:1332770^[3]	IDA: Inferred from Direct Assay		F
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0016020	membrane	PMID:17050691^[4]	IDA: Inferred from Direct Assay		C
	GO:0016491	oxidoreductase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0560	F
	GO:0016491	oxidoreductase activity	PMID:10423253^[5]	IDA: Inferred from Direct Assay		F
	GO:0022900	electron transport chain	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0249	P
	GO:0022900	electron transport chain	PMID:1332770^[3]	IDA: Inferred from Direct Assay		P
	GO:0043783	oxidoreductase activity, oxidizing metal ions with flavin as acceptor	PMID:4052375^[1]	IDA: Inferred from Direct Assay		F
	GO:0044429	mitochondrial part	PMID:10423253^[5]	IDA: Inferred from Direct Assay		C
	GO:0044429	mitochondrial part	PMID:1332770^[3]	IDA: Inferred from Direct Assay		C
	GO:0044429	mitochondrial part	PMID:1991113^[6]	IDA: Inferred from Direct Assay		C
	GO:0044429	mitochondrial part	PMID:4052375^[1]	IDA: Inferred from Direct Assay		C
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0048039	ubiquinone binding	PMID:17050691^[4]	IDA: Inferred from Direct Assay		F
	GO:0050660	flavin adenine dinucleotide binding	PMID:17050691^[4]	IDA: Inferred from Direct Assay		F
	GO:0051536	iron-sulfur cluster binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017896	F
	GO:0051536	iron-sulfur cluster binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0411	F
	GO:0051536	iron-sulfur cluster binding	PMID:17050691^[4]	IDA: Inferred from Direct Assay		F
	GO:0051536	iron-sulfur cluster binding	PMID:4052375^[1]	IDA: Inferred from Direct Assay		F
	GO:0051539	4 iron, 4 sulfur cluster binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0004	F
	GO:0051539	4 iron, 4 sulfur cluster binding	PMID:18037314^[7]	IDA: Inferred from Direct Assay		F
	GO:0055114	oxidation-reduction process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR007859	P
	GO:0055114	oxidation-reduction process	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0560	P
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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
↑ 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
↑ ^3.0 ^3.1 ^3.2 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
↑ ^4.0 ^4.1 ^4.2 ^4.3 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
↑ ^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
↑ 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:4052375-0] 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:9334218-1] 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:1332770-2] 3.0 ^3.1 ^3.2 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:17050691-3] 4.0 ^4.1 ^4.2 ^4.3 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:10423253-4] 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:1991113-5] 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:18037314-6] 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

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PIG:ETFD

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