1O94

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
F	d1o94f_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	ETFP subunits	Large, alpha subunit of electron transfer flavoprotein ETFP, N-terminal domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
D	d1o94d_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	ETFP subunits	Large, alpha subunit of electron transfer flavoprotein ETFP, N-terminal domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
A	d1o94a1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	FMN-linked oxidoreductases	FMN-linked oxidoreductases	Trimethylamine dehydrogenase, N-terminal domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
A	d1o94a2	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	C-terminal domain of adrenodoxin reductase-like	Trimethylamine dehydrogenase, C-terminal domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
A	d1o94a3	Alpha and beta proteins (a/b)	Nucleotide-binding domain	Nucleotide-binding domain	N-terminal domain of adrenodoxin reductase-like	Trimethylamine dehydrogenase, middle domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
B	d1o94b1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	FMN-linked oxidoreductases	FMN-linked oxidoreductases	Trimethylamine dehydrogenase, N-terminal domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
B	d1o94b2	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	C-terminal domain of adrenodoxin reductase-like	Trimethylamine dehydrogenase, C-terminal domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
B	d1o94b3	Alpha and beta proteins (a/b)	Nucleotide-binding domain	Nucleotide-binding domain	N-terminal domain of adrenodoxin reductase-like	Trimethylamine dehydrogenase, middle domain	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
C	d1o94c_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	ETFP subunits	Small, beta subunit of electron transfer flavoprotein ETFP	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)
E	d1o94e_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	ETFP subunits	Small, beta subunit of electron transfer flavoprotein ETFP	(Methylophilus methylotrophus ) [TaxId: 17 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
F	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8040144	3001593	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8040144	3001593	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thioredoxin reductase-like	8017579	3000050	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	FMN-linked oxidoreductases	8017577	3000014	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	FMN-linked oxidoreductases	8017577	3000014	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin reductase-like	8017579	3000050	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8040143	3001593	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8040143	3001593	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)
F	ETF	e1o94F1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: ETF	ECOD (1.6)
D	ETF	e1o94D1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: ETF	ECOD (1.6)
A	Oxidored_FMN	e1o94A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Oxidored_FMN	ECOD (1.6)
A	mycofact_OYE_2	e1o94A2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: mycofact_OYE_2	ECOD (1.6)
A	FAD_binding_3_1st	e1o94A3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Nucleotide-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
B	Oxidored_FMN	e1o94B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Oxidored_FMN	ECOD (1.6)
B	mycofact_OYE_2	e1o94B2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: mycofact_OYE_2	ECOD (1.6)
B	FAD_binding_3_1st	e1o94B3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Nucleotide-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
C	ETF	e1o94C1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: ETF	ECOD (1.6)
E	ETF	e1o94E1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: ETF	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
F	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
D	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
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)
B	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	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)
C	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
E	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
D, F	PF01012	Electron transfer flavoprotein domain (ETF)	Electron transfer flavoprotein domain	This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein [1].	Domain
A, B	PF00724	NADH:flavin oxidoreductase / NADH oxidase family (Oxidored_FMN)	NADH:flavin oxidoreductase / NADH oxidase family	-	Domain
A, B	PF22620	OYE-like second alpha/beta domain (OYE-like_second_a-b)	OYE-like second alpha/beta domain	This domain is found in a group of diverse dehydrogenases from the old yellow enzyme (OYE)-like family, such as histamine dehydrogenase from Nocardioides simplex, trimethylamine dehydrogenase from Methylophilus methylotrophus (sp. W(3)A(1)) and 2-nap ...	This domain is found in a group of diverse dehydrogenases from the old yellow enzyme (OYE)-like family, such as histamine dehydrogenase from Nocardioides simplex, trimethylamine dehydrogenase from Methylophilus methylotrophus (sp. W(3)A(1)) and 2-naphthoyl-CoA reductase (NCR) [1-4], which has been described as a small, second alpha/beta domain [3,4].	Domain
A, B	PF13450	NAD(P)-binding Rossmann-like domain (NAD_binding_8)	NAD(P)-binding Rossmann-like domain	-	Domain
C, E	PF01012	Electron transfer flavoprotein domain (ETF)	Electron transfer flavoprotein domain	This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
D, F	ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT	electron transfer activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	catabolic process oxoacid metabolic process organic acid catabolic process organic acid metabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation small molecule metabolic process lipid oxidation fatty acid metabolic process lipid catabolic process carboxylic acid metabolic process catabolic process oxoacid metabolic process organic acid catabolic process organic acid metabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation small molecule metabolic process lipid oxidation fatty acid metabolic process lipid catabolic process carboxylic acid metabolic process primary metabolic process lipid modification fatty acid catabolic process metabolic process cellular process monocarboxylic acid metabolic process small molecule catabolic process fatty acid beta-oxidation using acyl-CoA dehydrogenase lipid metabolic process	-
A, B	TRIMETHYLAMINE DEHYDROGENASE	binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors trimethylamine dehydrogenase activity binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors trimethylamine dehydrogenase activity catalytic activity oxidoreductase activity, acting on the CH-NH group of donors, flavin as acceptor iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding metal cluster binding cation binding metal ion binding	catabolic process metabolic process cellular process	-
C, E	ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding electron transfer activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
D, F	IPR014730	Electron transfer flavoprotein, alpha/beta-subunit, N-terminal	Domain
D, F	IPR001308	Electron transfer flavoprotein alpha subunit/FixB	Family
D, F	IPR014731	Electron transfer flavoprotein, alpha subunit, C-terminal	Domain
D, F	IPR029035	DHS-like NAD/FAD-binding domain superfamily	Homologous Superfamily
D, F	IPR018206	Electron transfer flavoprotein subunit alpha, conserved site	Conserved Site
D, F	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
D, F	IPR033947	Electron transfer flavoprotein, alpha subunit, N-terminal	Domain
A, B	IPR037348	TMADH/DMDH, FMN-binding domain	Domain
A, B	IPR001155	NADH:flavin oxidoreductase/NADH oxidase, N-terminal	Domain
A, B	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR051793	NADH:flavin oxidoreductase/NADH oxidase	Family
A, B	IPR054428	TMADH/DMDH/HD, second alpha/beta domain	Domain
C, E	IPR014730	Electron transfer flavoprotein, alpha/beta-subunit, N-terminal	Domain
C, E	IPR033948	Electron transfer flavoprotein, beta subunit, N-terminal	Domain
C, E	IPR000049	Electron transfer flavoprotein, beta-subunit, conserved site	Conserved Site
C, E	IPR012255	Electron transfer flavoprotein, beta subunit	Family
C, E	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily

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.