DB code: D00028

CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 Catalytic domain
E.C. 1.3.1.26
CSA 1arz
M-CSA 1arz
MACiE

CATH domain Related DB codes (homologues)
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 T00219 D00003 D00010 D00017 D00023 D00027 D00034 D00476
3.40.50.720 : Rossmann fold S00543 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P04036 Dihydrodipicolinate reductase
DHPR
EC 1.3.1.26
NP_414572.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488337.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF05173 (DapB_C)
PF01113 (DapB_N)
[Graphical View]

KEGG enzyme name
dihydrodipicolinate reductase
dihydrodipicolinic acid reductase
2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P04036 DAPB_ECOLI 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H. Homotetramer. Cytoplasm.

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

Compound table
Substrates Products Intermediates
KEGG-id C03972 C00006 C00003 C03340 C00004 C00005 C00080
E.C.
Compound 2,3,4,5-Tetrahydrodipicolinate NADP+ NAD+ 2,3-Dihydrodipicolinate NADH NADPH H+
Type carboxyl group,imine group amide group,amine group,nucleotide amide group,amine group,nucleotide aromatic ring (with nitrogen atoms),carboxyl group amide group,amine group,nucleotide amide group,amine group,nucleotide others
ChEBI 864
 864
 		18009
 18009
 		15846
 15846
 		18042
 18042
 		16908
 16908
 		16474
 16474
 		15378
 15378
PubChem 440179
 440179
 		5886
 5886
 		5893
 5893
 		439982
 439982
 		439153
 439153
 		5884
 5884
 		1038
 1038
1arzA01 Unbound Unbound Unbound Unbound Unbound Unbound
1arzB01 Unbound Unbound Bound:NAD Unbound Unbound Unbound
1arzC01 Unbound Unbound Bound:NAD Unbound Unbound Unbound
1arzD01 Unbound Unbound Bound:NAD Unbound Unbound Unbound
1dihA01 Unbound Unbound Unbound Unbound Unbound Bound:NDP
1druA01 Unbound Unbound Unbound Unbound Bound:NAD Unbound
1drvA01 Unbound Unbound Analogue:A3D Unbound Unbound Unbound
1drwA01 Unbound Unbound Analogue:NHD Unbound Unbound Unbound
1arzA02 Unbound Unbound Unbound Unbound Unbound Unbound
1arzB02 Unbound Unbound Unbound Analogue:PDC Unbound Unbound
1arzC02 Unbound Unbound Unbound Analogue:PDC Unbound Unbound
1arzD02 Unbound Unbound Unbound Analogue:PDC Unbound Unbound
1dihA02 Unbound Unbound Unbound Unbound Unbound Unbound
1druA02 Unbound Unbound Unbound Unbound Unbound Unbound
1drvA02 Unbound Unbound Unbound Unbound Unbound Unbound
1drwA02 Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1arzA01
1arzB01
1arzC01
1arzD01
1dihA01
1druA01
1drvA01
1drwA01
1arzA02 HIS 159;LYS 163
1arzB02 HIS 159;LYS 163
1arzC02 HIS 159;LYS 163
1arzD02 HIS 159;LYS 163
1dihA02 HIS 159;LYS 163
1druA02 HIS 159;LYS 163
1drvA02 HIS 159;LYS 163
1drwA02 HIS 159;LYS 163

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Scheme 3, p.3499-3500
[4]
Fig.4, p.15087-15088

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 95200850
PubMed ID 7893645
Journal Biochemistry
Year 1995
Volume 34
Pages 3502-12
Authors Scapin G, Blanchard JS, Sacchettini JC
Title Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase.
Related PDB
Related UniProtKB P04036
[2]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7893644
Journal Biochemistry
Year 1995
Volume 34
Pages 3492-501
Authors Reddy SG, Sacchettini JC, Blanchard JS
Title Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase.
Related PDB 1dih
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8873595
Journal Biochemistry
Year 1996
Volume 35
Pages 13294-302
Authors Reddy SG, Scapin G, Blanchard JS
Title Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.
Related PDB 1drw 1drv 1dru
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID 98060760
PubMed ID 9398235
Journal Biochemistry
Year 1997
Volume 36
Pages 15081-8
Authors Scapin G, Reddy SG, Zheng R, Blanchard JS
Title Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate.
Related PDB 1arz
Related UniProtKB P04036
[5]
Resource
Comments
Medline ID
PubMed ID 11342032
Journal Biochim Biophys Acta
Year 2001
Volume 1545
Pages 67-77
Authors Paiva AM, Vanderwall DE, Blanchard JS, Kozarich JW, Williamson JM, Kelly TM
Title Inhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-24 2009-02-26