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Reviewed, UniProtKB/Swiss-Prot P46829 (DAPB2_MYCBO)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydrodipicolinate reductase
      Short name=DHPR
    EC=1.3.1.26
Gene names
Name: dapB
OrganismMycobacterium bovis
Taxonomic identifier1765 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the dihydrodipicolinate reductase family.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

dihydrodipicolinate reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Dihydrodipicolinate reductase HAMAP MF_00102
PRO_0000141457

Sequences

Sequence LengthMass (Da)Tools
P46829-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 16DE4B090E481F6F

FASTA27127,679
        10         20         30         40         50         60 
MTTRVALVGG TGKLGAIIAG VIDELDDFET VAVLGSDERS REIDAADLVV DASTPGVSID 

        70         80         90        100        110        120 
VVRAAIERGK NVLVGTSGWS TERIALVRPL VEAAGTGAVF IPNFSLGSVV ATALAAAAAP 

       130        140        150        160        170        180 
LFPSIEIVET HRETKVDSPS GTAVRTAELI ADARVGVGPV ESPHVDQRAR GQQVASVPIH 

       190        200        210        220        230        240 
SLRRPGVIAN EETILSGPGE SLTIVHDTIE PARAYAPGIR IALAARADAR GVTIGLDALI 

       250        260        270 
DLGLAPRPAA PVIEVVDEGS VPGQVARVTG A 

« Hide

References

[1]"Genetic determination of the meso-diaminopimelate biosynthetic pathway of mycobacteria."
Cirillo J.D., Weisbrod T.R., Banerjee A., Bloom B.R., Jacobs W.R. Jr.
J. Bacteriol. 176:4424-4429(1994) [PubMed: 8021227] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BCG / Pasteur.

Cross-references

Sequence databases

L24366 Genomic DNA. Translation: AAA21562.1.
PIRA55517.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.1.26. 3091.

Family and domain databases

HAMAPMF_00102.
[Tree]
InterProIPR000846. DapB.
IPR011770. DapB_bac/pln.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR20836. DapB_bac/pln. 1 hit.
PfamPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
ProDomPD004105. DapB. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00036. dapB. 1 hit.
PROSITEPS01298. DAPB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPB2_MYCBO
AccessionPrimary (citable) accession number: P46829
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents