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Q9ZDR3 (ODPB_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit beta

EC=1.2.4.1
Gene names
Name:pdhB
Ordered Locus Names:RP262
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate By similarity.

Subunit structure

Heterodimer of an alpha and a beta chain.

Ontologies

Keywords
   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162227

Sites

Binding site591Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZDR3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 12A50A7ABBB28A46

FASTA32635,917
        10         20         30         40         50         60 
MQITVREALR DAMQEEMLRD EKVFVIGEEV AEYQGAYKVT QGLLEQFGSK RVIDTPITEY 

        70         80         90        100        110        120 
GFAGLAVGAA FAGLRPIVEF MTFNFAMQAF DHIVNSAAKT HYMSGGQVKC PIVFRGPNGA 

       130        140        150        160        170        180 
ASRVAAQHSQ NYTACYSHIP GLKVVAPYSA EDHKGLMLTA IRDDNPVIFL ENEILYGHSF 

       190        200        210        220        230        240 
DVPDIIEPIP FSKAKILKEG SNVTIVTFSI QVKLALDVVN ILQNDNIDCE LIDLRTIKPL 

       250        260        270        280        290        300 
DTDSIIESVK KTNRLVIVEE GWFFAGVGAS IASIVMKEAF DYLDAPIEIV SGKDVPLPYA 

       310        320 
VNLEKLAMPS ANDLIEAVKK VCYYSI 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235271 Genomic DNA. Translation: CAA14724.1.
PIRB71681.
RefSeqNP_220647.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZDR3.
SMRQ9ZDR3. Positions 1-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP262.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA14724; CAA14724; CAA14724.
GeneID883167.
KEGGrpr:RP262.
PATRIC17901284. VBIRicPro72556_0269.

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHOG000281450.
KOK00162.
OMADIPTPYN.
OrthoDBEOG6JQH4C.
ProtClustDBPRK09212.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPB_RICPR
AccessionPrimary (citable) accession number: Q9ZDR3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 13, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names