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Reviewed, UniProtKB/Swiss-Prot Q9X6Y9 (DAPB_BORPE)

Last modified November 4, 2008. Version 53. 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
Ordered Locus Names: BP2509
OrganismBordetella pertussis [Complete proteome] [HAMAP]
Taxonomic identifier520 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length269 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.

Pathway

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

Subcellular location

CytoplasmBy similarity.

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

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: HAMAP

   Molecular functiondihydrodipicolinate reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 269269Dihydrodipicolinate reductase
PRO_0000141415

Sequences

Sequence LengthMass (Da)Tools
Q9X6Y9-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 68DF3E7158BDAA31

FASTA26928,328
        10         20         30         40         50         60 
MTQATPQRIA IAGASGRMGQ MLIEAVLDTE GVELAVALDR AGSPSIGQDA GAALGRPCGV 

        70         80         90        100        110        120 
TITDQLDALA QADCLIDFTR PEGTLQHLQA CLRHDVKMVI GTTGFDSSGR AEIKVAAQKI 

       130        140        150        160        170        180 
AIVFAPNMSV GVNATLKLLD MAARILNSGY DVEIFEAHHR NKVDAPSGTA LIMGETVASA 

       190        200        210        220        230        240 
WDVALPDVAT WTRHGDTGVR KPGTIGFSVV RGGDIVGDHT VFFCGTGERI EISHRSSSRA 

       250        260 
TYAQGAVRAA RFLARQDNGL YDMQAVLGL 

« Hide

Cross-references

Sequence databases

AJ238308 Genomic DNA. Translation: CAB41012.1.
BX640418 Genomic DNA. Translation: CAE42781.1.
RefSeqNP_881136.1.

3D structure databases

HSSPHSSP built from PDB template 1DRW based on UniProtKB P04036.
ModBaseSearch...

Genome annotation databases

GeneID2665670.
GenomeReviewsGene locus BP2509 in contig BX470248_GR.
KEGGbpe:BP2509.
NMPDRfig|257313.1.peg.2210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9X6Y9.

Enzyme and pathway databases

BioCycBPER257313:BP2509-MON.

Family and domain databases

HAMAPMF_00102.
[Tree]
InterProIPR000846. DapB.
IPR011770. DapB_bac/pln.
IPR016040. NAD(P)-bd.
[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]
BLOCKSSearch...
ProtoNetSearch...

Entry information

Entry nameDAPB_BORPE
AccessionPrimary (citable) accession number: Q9X6Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 4, 2008
This is version 53 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