2GMJ

Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2gmja1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	Electron transfer flavoprotein-ubiquinone oxidoreductase, EFT-QO	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
A	d2gmja2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	Electron transfer flavoprotein-ubiquinone oxidoreductase-like	Electron transfer flavoprotein-ubiquinone oxidoreductase, EFT-QO	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
A	d2gmja3	Alpha and beta proteins (a+b)	Ferredoxin-like	4Fe-4S ferredoxins	ETF-QO domain-like	Electron transfer flavoprotein-ubiquinone oxidoreductase, EFT-QO	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d2gmjb1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	Electron transfer flavoprotein-ubiquinone oxidoreductase, EFT-QO	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d2gmjb2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	Electron transfer flavoprotein-ubiquinone oxidoreductase-like	Electron transfer flavoprotein-ubiquinone oxidoreductase, EFT-QO	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d2gmjb3	Alpha and beta proteins (a+b)	Ferredoxin-like	4Fe-4S ferredoxins	ETF-QO domain-like	Electron transfer flavoprotein-ubiquinone oxidoreductase, EFT-QO	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	4Fe-4S ferredoxins	8001550	3000020	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Flavoreductase-like	8001416	3000055	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Flavoreductase-like	8001416	3000055	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	4Fe-4S ferredoxins	8001550	3000020	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ETF_QO	e2gmjA1	A: a+b two layers	X: 4Fe-4S ferredoxin (From Topology)	H: 4Fe-4S ferredoxin (From Topology)	T: 4Fe-4S ferredoxin	F: ETF_QO	ECOD (1.6)
A	KOG2415	e2gmjA2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: KOG2415	ECOD (1.6)
A	FAD_binding_3_1st	e2gmjA3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
B	ETF_QO	e2gmjB1	A: a+b two layers	X: 4Fe-4S ferredoxin (From Topology)	H: 4Fe-4S ferredoxin (From Topology)	T: 4Fe-4S ferredoxin	F: ETF_QO	ECOD (1.6)
B	KOG2415	e2gmjB2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: KOG2415	ECOD (1.6)
B	FAD_binding_3_1st	e2gmjB3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A	3.30.9.90	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, domain 2	CATH (4.3.0)
A	3.30.70.20	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
B	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
B	3.30.9.90	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, domain 2	CATH (4.3.0)
B	3.30.70.20	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF21162	ETF-QO, ubiquinone-binding (ETFQO_UQ-bd)	ETF-QO, ubiquinone-binding	Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) is a a 4Fe4S flavoprotein located in the inner mitochondrial membrane and catalyses ubiquinone (UQ) reduction. It forms a single structural domain with three functional regions (that b ...	Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) is a a 4Fe4S flavoprotein located in the inner mitochondrial membrane and catalyses ubiquinone (UQ) reduction. It forms a single structural domain with three functional regions (that bind FAD, the 4Fe4S cluster, and UQ) which are closely packed and share structural elements [1]. This domain includes the residues involved in UQ binding [1]. This domain is also found in FixC proteins from bacteria, which share similarities with ETF-QO [2].	Domain
A, B	PF13450	NAD(P)-binding Rossmann-like domain (NAD_binding_8)	NAD(P)-binding Rossmann-like domain	-	Domain
A, B	PF05187	Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S (ETF_QO)	Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Electron transfer flavoprotein-ubiquinone oxidoreductase	oxidoreductase activity catalytic activity iron-sulfur cluster binding binding metal cluster binding small molecule binding flavin adenine dinucleotide binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding quinone binding oxidoreductase activity catalytic activity iron-sulfur cluster binding binding metal cluster binding small molecule binding flavin adenine dinucleotide binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding quinone binding ubiquinone binding electron transfer activity oxidoreductase activity, acting on the CH-NH group of donors electron-transferring-flavoprotein dehydrogenase activity oxidoreductase activity, acting on the CH-NH group of donors, quinone or similar compound as acceptor 4 iron, 4 sulfur cluster binding cation binding metal ion binding	electron transport chain metabolic process cellular process generation of precursor metabolites and energy response to oxidative stress response to stimulus response to stress	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR007859	ETF-QO/FixX, C-terminal domain	Domain
A, B	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR040156	Electron transfer flavoprotein-ubiquinone oxidoreductase	Family
A, B	IPR049398	ETF-QO/FixC, ubiquinone-binding	Domain
A, B	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain	Domain

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B	mpstruc	MONOTOPIC MEMBRANE PROTEINS	Oxidoreductases (Monotopic)	Electron Transfer Flavoprotein-ubiquinone oxidoreductase (ETF-QO) with bound UQ

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.