EzCatDB: D00028
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DB codeD00028
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
Domain 23.30.360.10 : Dihydrodipicolinate Reductase; domain 2Catalytic domain
E.C.1.3.1.26
CSA1arz

CATH domainRelated DB codes (homologues)
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2T00219,D00003,D00010,D00017,D00023,D00027,D00034,D00476
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

P04036
Protein nameDihydrodipicolinate reductasedihydrodipicolinate reductase
dihydrodipicolinic acid reductase
2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase
SynonymsDHPR
EC 1.3.1.26
RefSeqNP_414572.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488337.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF05173 (DapB_C)
PF01113 (DapB_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00300Lysine biosynthesis

UniProtKB:Accession NumberP04036
Entry nameDAPB_ECOLI
Activity2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H.
SubunitHomotetramer.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC03972C00006C00003C03340C00004C00005C00080
Compound2,3,4,5-TetrahydrodipicolinateNADP+NAD+2,3-DihydrodipicolinateNADHNADPHH+
Typecarboxyl group,imine groupamide group,amine group,nucleotideamide group,amine group,nucleotidearomatic ring (with nitrogen atoms),carboxyl groupamide group,amine group,nucleotideamide group,amine group,nucleotideothers
ChEBI864
18009
15846
18042
16908
16474
15378
PubChem440179
5886
5893
439982
439153
5884
1038
               
1arzA01UnboundUnboundUnboundUnboundUnboundUnbound 
1arzB01UnboundUnboundBound:NADUnboundUnboundUnbound 
1arzC01UnboundUnboundBound:NADUnboundUnboundUnbound 
1arzD01UnboundUnboundBound:NADUnboundUnboundUnbound 
1dihA01UnboundUnboundUnboundUnboundUnboundBound:NDP 
1druA01UnboundUnboundUnboundUnboundBound:NADUnbound 
1drvA01UnboundUnboundAnalogue:A3DUnboundUnboundUnbound 
1drwA01UnboundUnboundAnalogue:NHDUnboundUnboundUnbound 
1arzA02UnboundUnboundUnboundUnboundUnboundUnbound 
1arzB02UnboundUnboundUnboundAnalogue:PDCUnboundUnbound 
1arzC02UnboundUnboundUnboundAnalogue:PDCUnboundUnbound 
1arzD02UnboundUnboundUnboundAnalogue:PDCUnboundUnbound 
1dihA02UnboundUnboundUnboundUnboundUnboundUnbound 
1druA02UnboundUnboundUnboundUnboundUnboundUnbound 
1drvA02UnboundUnboundUnboundUnboundUnboundUnbound 
1drwA02UnboundUnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
literature [4]
pdbCatalytic residues
         
1arzA01 
1arzB01 
1arzC01 
1arzD01 
1dihA01 
1druA01 
1drvA01 
1drwA01 
1arzA02HIS 159;LYS 163
1arzB02HIS 159;LYS 163
1arzC02HIS 159;LYS 163
1arzD02HIS 159;LYS 163
1dihA02HIS 159;LYS 163
1druA02HIS 159;LYS 163
1drvA02HIS 159;LYS 163
1drwA02HIS 159;LYS 163

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Scheme 3, p.3499-3500
[4]Fig.4, p.15087-15088

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID95200850
PubMed ID7893645
JournalBiochemistry
Year1995
Volume34
Pages3502-12
AuthorsScapin G, Blanchard JS, Sacchettini JC
TitleThree-dimensional structure of Escherichia coli dihydrodipicolinate reductase.
Related UniProtKBP04036
[2]
CommentsX-ray crystallography
PubMed ID7893644
JournalBiochemistry
Year1995
Volume34
Pages3492-501
AuthorsReddy SG, Sacchettini JC, Blanchard JS
TitleExpression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase.
Related PDB1dih
[3]
PubMed ID8873595
JournalBiochemistry
Year1996
Volume35
Pages13294-302
AuthorsReddy SG, Scapin G, Blanchard JS
TitleInteraction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.
Related PDB1drw,1drv,1dru
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID98060760
PubMed ID9398235
JournalBiochemistry
Year1997
Volume36
Pages15081-8
AuthorsScapin G, Reddy SG, Zheng R, Blanchard JS
TitleThree-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate.
Related PDB1arz
Related UniProtKBP04036
[5]
PubMed ID11342032
JournalBiochim Biophys Acta
Year2001
Volume1545
Pages67-77
AuthorsPaiva AM, Vanderwall DE, Blanchard JS, Kozarich JW, Williamson JM, Kelly TM
TitleInhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis.


createdupdated
2004-03-242009-02-26


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