Annotations: 6N93

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6n93a_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Crotonase-like	Methylmalonyl CoA decarboxylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d6n93b_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Crotonase-like	Methylmalonyl CoA decarboxylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d6n93c_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Crotonase-like	Methylmalonyl CoA decarboxylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
D	d6n93d_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Crotonase-like	Methylmalonyl CoA decarboxylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
E	d6n93e_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Crotonase-like	Methylmalonyl CoA decarboxylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
F	d6n93f_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Crotonase-like	Methylmalonyl CoA decarboxylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ECH_1	e6n93A1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
B	ECH_1	e6n93B1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
C	ECH_1	e6n93C1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
D	ECH_1	e6n93D1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
E	ECH_1	e6n93E1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
F	ECH_1	e6n93F1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (utative)
A	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (utative)
B	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (utative)
B	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (utative)
C	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (utative)
C	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (utative)
D	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (utative)
D	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (utative)
E	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (utative)
E	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (utative)
F	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (utative)
F	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00378	Enoyl-CoA hydratase/isomerase (ECH_1)	Enoyl-CoA hydratase/isomerase	This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Methylmalonyl-CoA decarboxylase	methyl/ethyl malonyl-CoA decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity	fatty acid metabolic process lipid catabolic process catabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process lipid modification organic acid catabolic process organic acid metabolic process fatty acid catabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation fatty acid metabolic process lipid catabolic process catabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process lipid modification organic acid catabolic process organic acid metabolic process fatty acid catabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process lipid oxidation small molecule catabolic process lipid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR001753	Enoyl-CoA hydratase/isomerase	Family
A, B, C, D, E A, B, C, D, E, F	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR018376	Enoyl-CoA hydratase/isomerase, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR014748	Enoyl-CoA hydratase, C-terminal	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.