Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q92IS2 (ODPB_RICCN)

Last modified November 4, 2008. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Pyruvate dehydrogenase E1 component subunit beta
    EC=1.2.4.1
Gene names
Name: pdhB
Ordered Locus Names: RC0348
OrganismRickettsia conorii [Complete proteome] [HAMAP]
Taxonomic identifier781 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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 + CO(2).

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 processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162226

Sites

Binding site591Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92IS2-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 21A97CE0774EA9AE

FASTA32635,821
        10         20         30         40         50         60 
MQITVREALR DAMQEEMIRD DKVFVIGEEV AEYQGAYKVT QGLLEQFGPK RVIDTPITEY 

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

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

       190        200        210        220        230        240 
DVPKTIEPIP FGQAKILREG SSVTIVTFSI QVKLALDAAN FVQNDNIDCE VIDLRTIKPL 

       250        260        270        280        290        300 
DTETIIESVK KTNRLVVVEE GWFFAGVGAS IASIVMKEAF DYLDAPIEIV SGKDLPLPYA 

       310        320 
VNLETLALPS ESDVIEAVKK VCYYSI 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

AE008600 Genomic DNA. Translation: AAL02886.1.
PIRD97743.
RefSeqNP_359985.1.

3D structure databases

HSSPHSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
ModBaseSearch...

Genome annotation databases

GeneID928543.
GenomeReviewsGene locus RC0348 in contig AE006914_GR.
KEGGrco:RC0348.
NMPDRfig|272944.1.peg.348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ92IS2.

Enzyme and pathway databases

BioCycRCON272944:RC0348-MON.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR005475. Transketo_Cen_R.
IPR015941. Transketolase_C-like.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODPB_RICCN
AccessionPrimary (citable) accession number: Q92IS2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: November 4, 2008
This is version 43 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

Rickettsia conorii

(strain Malish 7): entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents