5ZMY

Crystal structure of a cis-epoxysuccinate hydrolase producing D(-)-tartaric acids

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Dihydropteroate synthetase-like	8059565	3000643	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	BKACE	e5zmyA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)
B	BKACE	e5zmyB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)
C	BKACE	e5zmyC1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)
D	BKACE	e5zmyD1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)
E	BKACE	e5zmyE1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)
F	BKACE	e5zmyF1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)
G	BKACE	e5zmyG1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)
H	BKACE	e5zmyH1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: BKACE	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF05853	beta-keto acid cleavage enzyme (BKACE)	beta-keto acid cleavage enzyme	BKACE, beta-keto acid cleavage enzyme plays, a role in lysine degradation. In certain instances it catalyses the conversion of 3-keto-5-aminohexanoate and acetyl-CoA into acetoacetate and 3-aminobutyryl-CoA [1]. The family is found to have at least 1 ...	BKACE, beta-keto acid cleavage enzyme plays, a role in lysine degradation. In certain instances it catalyses the conversion of 3-keto-5-aminohexanoate and acetyl-CoA into acetoacetate and 3-aminobutyryl-CoA [1]. The family is found to have at least 14 slightly different potential new enzymatic activities, all of which can therefore be designated as beta-keto acid cleavage enzymes [2].	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, G, H	Cis-epoxysuccinate hydrolase	hydrolase activity catalytic activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity 3-keto-5-aminohexanoate cleavage activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR008567	Beta-keto acid cleavage enzyme	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR013785	Aldolase-type TIM barrel	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.