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P0A0A3 (ODPB_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 41. 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
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Mass spectrometry

Molecular mass is 35230 Da from positions 1 - 325. Determined by MALDI. Ref.2

Ontologies

Keywords
   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processglycolytic process

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_0000162234

Sites

Binding site601Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A0A3 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 432ABDF6E4A720D5

FASTA32535,246
        10         20         30         40         50         60 
MAQMTMVQAI NDALKTELKN DQDVLIFGED VGVNGGVFRV TEGLQKEFGE DRVFDTPLAE 

        70         80         90        100        110        120 
SGIGGLAMGL AVEGFRPVME VQFLGFVFEV FDAIAGQIAR TRFRSGGTKT APVTIRSPFG 

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

       190        200        210        220        230        240 
REEVPEEEYT IDIGKANVKK EGNDISIITY GAMVQESMKA AEELEKDGYS VEVIDLRTVQ 

       250        260        270        280        290        300 
PIDVDTIVAS VEKTGRAVVV QEAQRQAGVG AAVVAELSER AILSLEAPIG RVAAADTIYP 

       310        320 
FTQAENVWLP NKNDIIEKAK ETLEF 

« Hide

References

[1]"Synthesis of pyruvate dehydrogenase is stimulated by osmotic stress in Staphylococcus aureus."
Vilhelmsson O., Miller K.J.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 12600 / IAM 12544 / NCTC 8532.
[2]"Identification of Staphylococcus aureus proteins recognized by the antibody-mediated immune response to a biofilm infection."
Brady R.A., Leid J.G., Camper A.K., Costerton J.W., Shirtliff M.E.
Infect. Immun. 74:3415-3426(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: MRSA-M2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF235026 Genomic DNA. Translation: AAF36410.1.

3D structure databases

ProteinModelPortalP0A0A3.
SMRP0A0A3. Positions 2-325.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP0A0A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0022.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProIPR029061. THDP-binding.
IPR009014. 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]
SUPFAMSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPB_STAAU
AccessionPrimary (citable) accession number: P0A0A3
Secondary accession number(s): Q9L6H5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: June 11, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program