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P40110 (DAPB_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrodipicolinate reductase

Short name=DHPR
EC=1.3.1.26
Gene names
Name:dapB
Ordered Locus Names:Cgl1973, cg2163
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-2,3,4,5-tetrahydrodipicolinate + NAD(P)+ = (S)-2,3-dihydrodipicolinate + NAD(P)H. HAMAP MF_00102

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP MF_00102

Subcellular location

Cytoplasm By similarity HAMAP MF_00102.

Sequence similarities

Belongs to the dihydrodipicolinate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Diaminopimelate biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADPH binding

Inferred from electronic annotation. Source: InterPro

dihydrodipicolinate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Dihydrodipicolinate reductase HAMAP MF_00102
PRO_0000141435

Experimental info

Sequence conflict911D → A in CAA79712. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P40110 [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: A0B143F478D12414

FASTA24826,024
        10         20         30         40         50         60 
MGIKVGVLGA KGRVGQTIVA AVNESDDLEL VAEIGVDDDL SLLVDNGAEV VVDFTTPNAV 

        70         80         90        100        110        120 
MGNLEFCINN GISAVVGTTG FDDARLEQVR DWLEGKDNVG VLIAPNFAIS AVLTMVFSKQ 

       130        140        150        160        170        180 
AARFFESAEV IELHHPNKLD APSGTAIHTA QGIAAARKEA GMDAQPDATE QALEGSRGAS 

       190        200        210        220        230        240 
VDGIPVHAVR MSGMVAHEQV IFGTQGQTLT IKQDSYDRNS FAPGVLVGVR NIAQHPGLVV 


GLEHYLGL 

« Hide

References

« Hide 'large scale' references
[1]Eikmanns B.J., Eggeling L., Thum-Schmitz N., Krumbach K.
Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"A cluster of three genes (dapA, orf2, and dapB) of Brevibacterium lactofermentum encodes dihydrodipicolinate synthase, dihydrodipicolinate reductase, and a third polypeptide of unknown function."
Pisabarro A., Malumbres M., Mateos L.M., Oguiza J.A., Martin J.F.
J. Bacteriol. 175:2743-2749(1993) [PubMed: 8478336] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
[3]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67737 Genomic DNA. Translation: CAA47968.1.
Z21502 Genomic DNA. Translation: CAA79712.1.
BA000036 Genomic DNA. Translation: BAB99366.1.
BX927153 Genomic DNA. Translation: CAF20314.1.
PIRA40626.
RefSeqNP_601179.1. NC_003450.3.
YP_226215.1. NC_006958.1.

3D structure databases

ProteinModelPortalP40110.
SMRP40110. Positions 3-248.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019930.
3345049.
GenomeReviewsGene locus Cgl1973 in contig BA000036_GR.
Gene locus cg2163 in contig BX927147_GR.
KEGGcgb:cg2163.
cgl:NCgl1898.
PATRIC21495948. VBICorGlu203724_1910.

Phylogenomic databases

HOGENOMHBG594002.
OMADRASFMP.
PhylomeDBP40110.
ProtClustDBPRK00048.

Enzyme and pathway databases

BioCycCGLU196627:CG2163-MONOMER.
MetaCyc:MONOMER-6445.

Family and domain databases

HAMAPMF_00102. DapB.
[Tree]
InterProIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR011770. Dihydrodipicolinate_Rdtase.
IPR023940. Dihydrodipicolinate_Rdtase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00215.
PANTHERPTHR20836. DapB_bac/pln. 1 hit.
PfamPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFPIRSF000161. DHPR. 1 hit.
TIGRFAMsTIGR00036. DapB. 1 hit.
PROSITEPS01298. DAPB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPB_CORGL
AccessionPrimary (citable) accession number: P40110
Secondary accession number(s): P42462
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 11, 2001
Last modified: January 25, 2012
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families