3CJ8

Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase from Enterococcus faecalis V583

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00132	e3cj8A3	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: PF00132	ECOD (1.6)
A	PF08503	e3cj8A2	A: a+b two layers	X: Alpha-beta plaits	H: Tetrahydrodipicolinate acetyltransferase N-terminal domain (From Topology)	T: Tetrahydrodipicolinate acetyltransferase N-terminal domain	F: PF08503	ECOD (1.6)
C	PF00132	e3cj8C2	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: PF00132	ECOD (1.6)
C	PF08503	e3cj8C1	A: a+b two layers	X: Alpha-beta plaits	H: Tetrahydrodipicolinate acetyltransferase N-terminal domain (From Topology)	T: Tetrahydrodipicolinate acetyltransferase N-terminal domain	F: PF08503	ECOD (1.6)
B	PF00132	e3cj8B2	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: PF00132	ECOD (1.6)
B	PF08503	e3cj8B1	A: a+b two layers	X: Alpha-beta plaits	H: Tetrahydrodipicolinate acetyltransferase N-terminal domain (From Topology)	T: Tetrahydrodipicolinate acetyltransferase N-terminal domain	F: PF08503	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	4.10.180.10	Few Secondary Structures	Irregular	Black beetle virus capsid protein		CATH (4.3.0)
A	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (4.3.0)
A	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)
C	4.10.180.10	Few Secondary Structures	Irregular	Black beetle virus capsid protein		CATH (4.3.0)
C	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (4.3.0)
C	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)
B	4.10.180.10	Few Secondary Structures	Irregular	Black beetle virus capsid protein		CATH (4.3.0)
B	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (4.3.0)
B	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00132	Bacterial transferase hexapeptide (six repeats) (Hexapep)	Bacterial transferase hexapeptide (six repeats)	-	Repeat
A, B, C	PF08503	Tetrahydrodipicolinate succinyltransferase N-terminal (DapH_N)	Tetrahydrodipicolinate succinyltransferase N-terminal	-	Family
A, B, C	PF14602	Hexapeptide repeat of succinyl-transferase (Hexapep_2)	Hexapeptide repeat of succinyl-transferase	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase	acetyltransferase activity N-acetyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity tetrahydrodipicolinate N-acetyltransferase activity catalytic activity N-acyltransferase activity	diaminopimelate biosynthetic process oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process lipid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process dicarboxylic acid biosynthetic process organonitrogen compound metabolic process diaminopimelate biosynthetic process oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process lipid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process dicarboxylic acid biosynthetic process organonitrogen compound metabolic process small molecule biosynthetic process cellular metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process fatty acid derivative biosynthetic process primary metabolic process fatty acid derivative metabolic process diaminopimelate metabolic process amino acid biosynthetic process biosynthetic process metabolic process cellular process lipid metabolic process lysine metabolic process aspartate family amino acid biosynthetic process aspartate family amino acid metabolic process alpha-amino acid metabolic process lysine biosynthetic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process lysine biosynthetic process via diaminopimelate proteinogenic amino acid biosynthetic process alpha-amino acid biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR013710	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase, N-terminal	Domain
A, B, C	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A, B, C	IPR019873	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase, DapH	Family
A, B, C	IPR018357	Hexapeptide transferase, conserved site	Conserved Site
A, B, C	IPR001451	Hexapeptide repeat	Repeat

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 R01GM133198.