EzCatDB: D00094
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DB codeD00094
CATH domainDomain 11.10.166.10 : Tetrahydrodipicolinate-N-succinyltransferase; Chain A, domain 1
Domain 22.160.10.10 : UDP N-Acetylglucosamine Acyltransferase; domain 1Catalytic domain
E.C.2.3.1.117
CSA2tdt

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

Enzyme Name
UniProtKBKEGG

P56220
Protein name2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase2,3,4,5-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
SynonymsEC 2.3.1.117
Tetrahydrodipicolinate N-succinyltransferase
THP succinyltransferase
Tetrahydropicolinate succinylase
PfamPF00132 (Hexapep)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00300Lysine biosynthesis

UniProtKB:Accession NumberP56220
Entry nameDAPD_MYCBO
ActivitySuccinyl-CoA + (S)-2,3,4,5-tetrahydropyridine- 2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6- oxoheptanedioate.
SubunitHomotrimer.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00091C03972C00001C00010C04462
CompoundSuccinyl-CoA2,3,4,5-TetrahydrodipicolinateH2OCoAN-Succinyl-L-2-amino-6-oxoheptanedioate
Typeamine group,carbohydrate,carboxyl group,nucleotide,peptide/protein,sulfide groupcarboxyl group,imine groupH2Oamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl groupamino acids,amide group,carbohydrate,carboxyl group
ChEBI15380
864
15377
15346
35266

PubChem92133
439161
440179
962
22247451
87642
6816
440349

              
1tdtA01UnboundUnbound UnboundUnboundUnbound
1tdtB01UnboundUnbound UnboundUnboundUnbound
1tdtC01UnboundUnbound UnboundUnboundUnbound
2tdtA01UnboundUnbound UnboundUnboundUnbound
3tdtA01UnboundUnbound UnboundUnboundUnbound
1tdtA02UnboundUnbound UnboundUnboundUnbound
1tdtB02UnboundUnbound UnboundUnboundUnbound
1tdtC02UnboundUnbound UnboundUnboundUnbound
2tdtA02UnboundUnbound Bound:COAUnboundIntermediate-analogue:NPI
3tdtA02UnboundUnbound Bound:COAUnboundBound:26P

Active-site residues
resource
literature [3]
pdbCatalytic residues
         
1tdtA01 
1tdtB01 
1tdtC01 
2tdtA01 
3tdtA01 
1tdtA02ASP 141
1tdtB02ASP 141
1tdtC02ASP 141
2tdtA02ASP 141
3tdtA02ASP 141

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.10368-10369
[5]p.975-978

references
[1]
PubMed ID8880935
JournalProteins
Year1996
Volume26
Pages115-7
AuthorsBinder DA, Blanchard JS, Roderick SL
TitleCrystallization and preliminary crystallographic analysis of tetrahydrodipicolinate-N-succinyltransferase.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID97164902
PubMed ID9012664
JournalBiochemistry
Year1997
Volume36
Pages489-94
AuthorsBeaman TW, Binder DA, Blanchard JS, Roderick SL
TitleThree-dimensional structure of tetrahydrodipicolinate N-succinyltransferase.
Related PDB1tdt
Related UniProtKBP56220
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID98337777
PubMed ID9671504
JournalBiochemistry
Year1998
Volume37
Pages10363-9
AuthorsBeaman TW, Blanchard JS, Roderick SL
TitleThe conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase.
Related PDB2tdt,3tdt
Related UniProtKBP56220
[4]
PubMed ID11106178
JournalProtein Sci
Year2000
Volume9
Pages2034-7
AuthorsCirilli M, Scapin G, Sutherland A, Vederas JC, Blanchard JS
TitleThe three-dimensional structure of the ternary complex of Corynebacterium glutamicum diaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate.
[5]
PubMed ID11910040
JournalProtein Sci
Year2002
Volume11
Pages974-9
AuthorsBeaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL
TitleAcyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.


createdupdated
2004-03-172009-02-26


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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