Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q63QT3 (DAPB_BURPS)

Last modified November 25, 2008. Version 31. 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: BPSL2941
OrganismBurkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]
Taxonomic identifier28450 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length268 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 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 – 268268Dihydrodipicolinate reductase
PRO_0000228333

Sequences

Sequence LengthMass (Da)Tools
Q63QT3-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 6CD0F6B0DAE082A3

FASTA26828,136
        10         20         30         40         50         60 
MSSMKIAIAG ASGRMGRMLI EAVLAAPDAT LAGALDRTGS PQLGQDAGAF LGKQTGVALT 

        70         80         90        100        110        120 
DDIERVCAEA DYLIDFTRPE GTLAHLDAAL RHDVKLVIGT TGFSEPQKAQ LRAAGGKIAL 

       130        140        150        160        170        180 
VFSANMSVGV NVTMKLLEFA AKQFAQGYDI EIIEAHHRHK VDAPSGTALM MGETIAAATG 

       190        200        210        220        230        240 
RTLDDCAVYG RHGVTGERDP STIGFSAIRG GDIVGDHTVL FAGIGERIEI THKSASRVSY 

       250        260 
AQGALRAARF LAGHQAGFFD MQDVLGLR 

« Hide

Cross-references

Sequence databases

BX571965 Genomic DNA. Translation: CAH36951.1.
RefSeqYP_109535.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3094347.
GenomeReviewsGene locus BPSL2941 in contig BX571965_GR.
KEGGbps:BPSL2941.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ63QT3.

Enzyme and pathway databases

BioCycBPSE272560:BPSL2941-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. 2 hits.
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 nameDAPB_BURPS
AccessionPrimary (citable) accession number: Q63QT3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 25, 2004
Last modified: November 25, 2008
This is version 31 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