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B0BWB9 (B0BWB9_RICRO) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102

Short name=HTPA reductase HAMAP-Rule MF_00102
EC=1.17.1.8 HAMAP-Rule MF_00102
Gene names
Name:dapB HAMAP-Rule MF_00102
Ordered Locus Names:RrIowa_0233 EMBL ABY72145.1
OrganismRickettsia rickettsii (strain Iowa) [Complete proteome] [HAMAP] EMBL ABY72145.1
Taxonomic identifier452659 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate By similarity. HAMAP-Rule MF_00102 SAAS SAAS023940

Catalytic activity

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H. HAMAP-Rule MF_00102 SAAS SAAS023940

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP-Rule MF_00102 SAAS SAAS023940

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00102

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00102 SAAS SAAS023940.

Sequence similarities

Belongs to the DapB family. HAMAP-Rule MF_00102

Caution

Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli (PubMed:20503968) that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. HAMAP-Rule MF_00102

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding54 – 596NAD(P) By similarity HAMAP-Rule MF_00102
Nucleotide binding124 – 1263NAD(P) By similarity HAMAP-Rule MF_00102
Nucleotide binding148 – 1514NAD(P) By similarity HAMAP-Rule MF_00102
Region190 – 1912Substrate binding By similarity HAMAP-Rule MF_00102

Sites

Active site1801Proton donor/acceptor By similarity HAMAP-Rule MF_00102
Active site1841Proton donor By similarity HAMAP-Rule MF_00102
Binding site1811Substrate By similarity HAMAP-Rule MF_00102

Sequences

Sequence LengthMass (Da)Tools
B0BWB9 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 549827E6CE4F0EA0

FASTA28531,820
        10         20         30         40         50         60 
MASYNKICGS NYIKYTLRSK DFRRLALVQI KLRLLTVHLL GVYIANMLNI GLSGSTGKMG 

        70         80         90        100        110        120 
ETILERIDKF KDCKIAAKFN STNNLDDLDN FCKNSDVIID FSTPEILEKL INYALKHNTK 

       130        140        150        160        170        180 
LVIGTTGLQP QHFKLLEKAA QTLPVLYSAN MSIGANLLSY LAKEVTKILD DYDVEILETH 

       190        200        210        220        230        240 
HRNKKDSPSG TAVMLAETIA SKKGLNITFN RGNRLRSEKE IGISSLRGGN VHGIHEISFL 

       250        260        270        280 
GDDEIITLKH EALNKNSFSI GAIKAAIWLQ DKPSALYSMQ DIYKI 

« Hide

References

[1]"Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and avirulent Rickettsia rickettsii Iowa."
Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F., Hackstadt T.
Infect. Immun. 76:542-550(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Iowa EMBL ABY72145.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000766 Genomic DNA. Translation: ABY72145.1.
RefSeqYP_001649551.1. NC_010263.2.

3D structure databases

ProteinModelPortalB0BWB9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING452659.RrIowa_0233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY72145; ABY72145; RrIowa_0233.
GeneID5849763.
KEGGrrj:RrIowa_0233.
PATRIC17906348. VBIRicRic59104_0227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0289.
HOGENOMHOG000227155.
KOK00215.
OMAAHHRFKV.
OrthoDBEOG6SV5DS.

Enzyme and pathway databases

BioCycRRIC452659:GHSN-224-MONOMER.
UniPathwayUPA00034; UER00018.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00102. DapB.
InterProIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR011770. Dihydrodipicolinate_Rdtase.
IPR023940. Dihydrodipicolinate_Rdtase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR20836. PTHR20836. 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 nameB0BWB9_RICRO
AccessionPrimary (citable) accession number: B0BWB9
Entry history
Integrated into UniProtKB/TrEMBL: February 26, 2008
Last sequence update: February 26, 2008
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)