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Q5HQ75 (ODPB_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 62. 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:
Pyruvate dehydrogenase E1 component subunit beta

EC=1.2.4.1
Gene names
Name:pdhB
Ordered Locus Names:SERP0681
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

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_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 – 325325Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162236

Sites

Binding site601Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HQ75 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 01A6E5FB2D9C1CCE

FASTA32535,293
        10         20         30         40         50         60 
MAQMTMVQAI NDALKSELKR DEDVLVFGED VGVNGGVFRV TEGLQKEFGE DRVFDTPLAE 

        70         80         90        100        110        120 
SGIGGLALGL AVTGFRPVME IQFLGFVYEV FDEVAGQIAR TRFRSGGTKP APVTIRTPFG 

       130        140        150        160        170        180 
GGVHTPELHA DNLEGILAQS PGLKVVIPSG PYDAKGLLIS SIQSNDPVVY LEHMKLYRSF 

       190        200        210        220        230        240 
REEVPEEEYK IDIGKANVKK EGNDITLISY GAMVQESLKA AEELEKDGYS VEVIDLRTVQ 

       250        260        270        280        290        300 
PIDIDTLVAS VEKTGRAVVV QEAQRQAGVG AQVAAELAER AILSLEAPIA RVAASDTIYP 

       310        320 
FTQAENVWLP NKKDIIEQAK ATLEF 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54053.1.
RefSeqYP_188265.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HQ75.
SMRQ5HQ75. Positions 2-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0681.

Proteomic databases

PRIDEQ5HQ75.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54053; AAW54053; SERP0681.
GeneID3240396.
KEGGser:SERP0681.
PATRIC19612231. VBIStaEpi130894_0659.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHOG000281451.
KOK00162.
OMAHAQEWDY.
OrthoDBEOG6JQH4C.
ProtClustDBCLSK885133.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-706-MONOMER.

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_STAEQ
AccessionPrimary (citable) accession number: Q5HQ75
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: November 13, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program