Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1RJX3 (ODPB_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 50. 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:RBE_0260
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length325 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
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process from pyruvate

Inferred from electronic annotation. Source: InterPro

glycolysis

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 – 325325Pyruvate dehydrogenase E1 component subunit beta
PRO_0000288760

Sites

Binding site591Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RJX3 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 89AC46026246C64B

FASTA32535,708
        10         20         30         40         50         60 
MQITVREALR DAMQEEMIRD DKVFVMGEEV AEYQGAYKVT QGLLEQFGPK RVIDTPITEY 

        70         80         90        100        110        120 
GFAGLAVGAA FAGLRPIVEF MTFNFAMQAM DHIVNSAAKT HYMSGGQVRC PIVFRGPNGA 

       130        140        150        160        170        180 
ASRVAAQHSQ NYAACYSYIP GLKVVAPYSA EDHKGLMITA IRDDNPVIFL ENEILYGHSF 

       190        200        210        220        230        240 
DISENVEPIP FGKAKVLKEG DSVTIVTFSI QVKLALDAAN ILQSDNINCE VIDLRTIKPL 

       250        260        270        280        290        300 
DIDTIIESVK KTGRLVVIEE GWFFAGIGAT IAAIVMKEAF DYLDAPVEIV SGKDVPLPYA 

       310        320 
VNLEKLALPS EYDVINAVKK VCYIK 

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000087 Genomic DNA. Translation: ABE04341.1.
RefSeqYP_537430.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RJX3.
SMRQ1RJX3. Positions 1-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_0260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04341; ABE04341; RBE_0260.
GeneID3995884.
KEGGrbe:RBE_0260.
PATRIC17881833. VBIRicBel102610_0296.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRBEL336407:GJCY-266-MONOMER.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR027110. PDHB.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERPTHR11624:SF11. PTHR11624:SF11. 1 hit.
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_RICBR
AccessionPrimary (citable) accession number: Q1RJX3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 16, 2006
Last modified: November 13, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names