DB code: D00094

CATH domain 1.10.166.10 : Tetrahydrodipicolinate-N-succinyltransferase; Chain A, domain 1
2.160.10.10 : UDP N-Acetylglucosamine Acyltransferase; domain 1 Catalytic domain
E.C. 2.3.1.117
CSA 2tdt
M-CSA 2tdt
MACiE

CATH domain Related DB codes (homologues)
2.160.10.10 : UDP N-Acetylglucosamine Acyltransferase; domain 1 D00464 S00167 D00417

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P56220 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
EC 2.3.1.117
Tetrahydrodipicolinate N-succinyltransferase
THP succinyltransferase
Tetrahydropicolinate succinylase
PF00132 (Hexapep)
[Graphical View]

KEGG enzyme name
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
tetrahydropicolinate succinylase
tetrahydrodipicolinate N-succinyltransferase
tetrahydrodipicolinate succinyltransferase
succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase
succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylateN-succinyltransferase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P56220 DAPD_MYCBO Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine- 2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6- oxoheptanedioate. Homotrimer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00300 Lysine biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C00091 C03972 C00001 C00010 C04462
E.C.
Compound Succinyl-CoA 2,3,4,5-Tetrahydrodipicolinate H2O CoA N-Succinyl-L-2-amino-6-oxoheptanedioate
Type amine group,carbohydrate,carboxyl group,nucleotide ,peptide/protein,sulfide group carboxyl group,imine group H2O amine group,carbohydrate,nucleotide ,peptide/protein,sulfhydryl group amino acids,amide group,carbohydrate,carboxyl group
ChEBI 15380
864
15377
15346
35266
PubChem 439161
92133
440179
22247451
962
6816
87642
440349
1tdtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1tdtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1tdtC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2tdtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3tdtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1tdtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1tdtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1tdtC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2tdtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:COA Unbound Intermediate-analogue:NPI
3tdtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:COA Unbound Bound:26P

Reference for Active-site residues
resource references E.C.
literature [3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1tdtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1tdtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1tdtC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2tdtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tdtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1tdtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 141
1tdtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 141
1tdtC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 141
2tdtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 141
3tdtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 141

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.10368-10369
[5]
p.975-978

References
[1]
Resource
Comments
Medline ID
PubMed ID 8880935
Journal Proteins
Year 1996
Volume 26
Pages 115-7
Authors Binder DA, Blanchard JS, Roderick SL
Title Crystallization and preliminary crystallographic analysis of tetrahydrodipicolinate-N-succinyltransferase.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 97164902
PubMed ID 9012664
Journal Biochemistry
Year 1997
Volume 36
Pages 489-94
Authors Beaman TW, Binder DA, Blanchard JS, Roderick SL
Title Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase.
Related PDB 1tdt
Related UniProtKB P56220
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 98337777
PubMed ID 9671504
Journal Biochemistry
Year 1998
Volume 37
Pages 10363-9
Authors Beaman TW, Blanchard JS, Roderick SL
Title The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase.
Related PDB 2tdt 3tdt
Related UniProtKB P56220
[4]
Resource
Comments
Medline ID
PubMed ID 11106178
Journal Protein Sci
Year 2000
Volume 9
Pages 2034-7
Authors Cirilli M, Scapin G, Sutherland A, Vederas JC, Blanchard JS
Title The three-dimensional structure of the ternary complex of Corynebacterium glutamicum diaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11910040
Journal Protein Sci
Year 2002
Volume 11
Pages 974-9
Authors Beaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL
Title Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-17 2009-02-26