1HUX

CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A

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)
A	d1huxa_	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Actin-like ATPase domain	BadF/BadG/BcrA/BcrD-like	Hydroxyglutaryl-CoA dehydratase component A	(Acidaminococcus fermentans ) [TaxId: 905 ],	SCOPe (2.08)
B	d1huxb_	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Actin-like ATPase domain	BadF/BadG/BcrA/BcrD-like	Hydroxyglutaryl-CoA dehydratase component A	(Acidaminococcus fermentans ) [TaxId: 905 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	BadF/BadG/BcrA/BcrD-like	8020938	4003392	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Actin-like ATPases	8033318	3000092	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Actin-like ATPases	8092409	3000092	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Actin-like ATPases	8092409	3000092	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Actin-like ATPases	8033318	3000092	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	PF01869	e1huxA2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF01869	ECOD (1.6)
B	PF01869	e1huxB3	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF01869	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.420.40	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
B	3.30.420.40	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01869	BadF/BadG/BcrA/BcrD ATPase family (BcrAD_BadFG)	BadF/BadG/BcrA/BcrD ATPase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	ACTIVATOR OF (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding metal cluster binding cation binding metal ion binding	catabolic process oxoacid metabolic process energy derivation by oxidation of organic compounds glutamine family amino acid catabolic process glutamate catabolic process via 2-hydroxyglutarate amino acid metabolic process organic acid metabolic process dicarboxylic acid catabolic process organic acid catabolic process alpha-amino acid metabolic process anaerobic glutamate catabolic process fermentation glutamine family amino acid metabolic process cellular catabolic process organic substance metabolic process catabolic process oxoacid metabolic process energy derivation by oxidation of organic compounds glutamine family amino acid catabolic process glutamate catabolic process via 2-hydroxyglutarate amino acid metabolic process organic acid metabolic process dicarboxylic acid catabolic process organic acid catabolic process alpha-amino acid metabolic process anaerobic glutamate catabolic process fermentation glutamine family amino acid metabolic process cellular catabolic process organic substance metabolic process nitrogenous compound fermentation carboxylic acid catabolic process glutamate metabolic process small molecule metabolic process amino acid catabolic process organonitrogen compound catabolic process glutamate catabolic process organonitrogen compound metabolic process cellular metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process generation of precursor metabolites and energy L-amino acid metabolic process anaerobic amino acid catabolic process proteinogenic amino acid metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process organic substance catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002731	ATPase, BadF/BadG/BcrA/BcrD type	Domain
A, B	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
A, B	IPR008275	Acyl-CoA dehydratase activase domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.