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
15380
864
864
15377
15377
15346
15346
35266
35266
PubChem 439161
92133
439161
92133
440179
440179
22247451
962
22247451
962
6816
87642
6816
87642
440349
440349
1tdtA01 Unbound Unbound Unbound Unbound Unbound
1tdtB01 Unbound Unbound Unbound Unbound Unbound
1tdtC01 Unbound Unbound Unbound Unbound Unbound
2tdtA01 Unbound Unbound Unbound Unbound Unbound
3tdtA01 Unbound Unbound Unbound Unbound Unbound
1tdtA02 Unbound Unbound Unbound Unbound Unbound
1tdtB02 Unbound Unbound Unbound Unbound Unbound
1tdtC02 Unbound Unbound Unbound Unbound Unbound
2tdtA02 Unbound Unbound Bound:COA Unbound Intermediate-analogue:NPI
3tdtA02 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
1tdtB01
1tdtC01
2tdtA01
3tdtA01
1tdtA02 ASP 141
1tdtB02 ASP 141
1tdtC02 ASP 141
2tdtA02 ASP 141
3tdtA02 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