DB code: D00094
CATH domain | 1.10.166.10 : Tetrahydrodipicolinate-N-succinyltransferase; Chain A, domain 1 | |
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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) |
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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 |
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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 | ||
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References | Sections | No. of steps in catalysis |
[3]
|
p.10368-10369 | |
[5]
|
p.975-978 |
References | |
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[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 |
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Created | Updated |
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2004-03-17 | 2009-02-26 |