2TDT

COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINOPIMELATE AND COENZYME 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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2tdta_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Tetrahydrodipicolinate-N-succinlytransferase, THDP-succinlytransferase, DapD	Tetrahydrodipicolinate-N-succinlytransferase, THDP-succinlytransferase, DapD	(Mycobacterium tuberculosis variant bovis ) [TaxId: 1765 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8042987	3001804	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	Hexapep_2_1	e2tdtA1	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: Hexapep_2_1	ECOD (1.6)
A	THDPS_N_2	e2tdtA2	A: alpha arrays	X: Tetrahydrodipicolinate-N-succinlytransferase, N-terminal 3-helical domain (From Topology)	H: Tetrahydrodipicolinate-N-succinlytransferase, N-terminal 3-helical domain (From Topology)	T: Tetrahydrodipicolinate-N-succinlytransferase, N-terminal 3-helical domain	F: THDPS_N_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.166.10	Mainly Alpha	Orthogonal Bundle	Tetrahydrodipicolinate-N-succinyltransferase	Chain A, domain 1	CATH (4.3.0)
A	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	PF14805	Tetrahydrodipicolinate N-succinyltransferase N-terminal (THDPS_N_2)	Tetrahydrodipicolinate N-succinyltransferase N-terminal	This is the N-terminal domain of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase [1].	Domain
A	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	TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE	N-succinyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity succinyltransferase 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	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR023180	Tetrahydrodipicolinate-N-succinyltransferase, chain A, domain 1	Domain
A	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A	IPR005664	Tetrahydrodipicolinate N-succinyltransferase, transferase hexapeptide repeat family	Family
A	IPR018357	Hexapeptide transferase, conserved site	Conserved Site
A	IPR037133	Tetrahydrodipicolinate-N-succinyltransferase, N-terminal domain superfamily	Homologous Superfamily
A	IPR001451	Hexapeptide repeat	Repeat

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase M-CSA #932	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (also known as tetrahydrodipicolinate N-succinyltransferase or DapD) is part of the succinyl route of of lysine/diaminopimelic acid (DAP) biosynthesis. DAP biosynthesis is one of the two lysine biosynthesis pathways that are known to have evolved.	Defined by 3 residues: ASP:A_3-141GLY:A_2-166GLU:A_2-189 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.3.1.117 (PDB Primary Data) Search M-CSA Motif + EC 2.3.1.117

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.