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Reviewed, UniProtKB/Swiss-Prot Q62H17 (DAPB_BURMA)

Last modified June 16, 2009. Version 33. 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: BMA2456
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [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. 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
   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: 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 – 268268Dihydrodipicolinate reductase HAMAP MF_00102
PRO_0000228332

Sequences

Sequence LengthMass (Da)Tools
Q62H17-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 51A521ED19C34F61

FASTA26828,126
        10         20         30         40         50         60 
MSSMKIAIAG ASGRMGRMLI EAVLAAPDAT LAGALDRTGS SQLGQDAGAF 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

CP000010 Genomic DNA. Translation: AAU49702.1.
RefSeqYP_104003.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3089894.
GenomeReviewsGene locus BMA2456 in contig CP000010_GR.
KEGGbma:BMA2456.
TIGRBMA2456.

Phylogenomic databases

HOGENOMQ62H17.
OMAQ62H17. TIGFSTI.

Enzyme and pathway databases

BioCycBMAL243160:BMA_2456-MON.
BRENDA1.3.1.26. 260531.

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. 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_BURMA
AccessionPrimary (citable) accession number: Q62H17
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 25, 2004
Last modified: June 16, 2009
This is version 33 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