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P0A0A3

- ODPB_STAAU

UniProt

P0A0A3 - ODPB_STAAU

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Protein
Pyruvate dehydrogenase E1 component subunit beta
Gene
pdhB
Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Thiamine pyrophosphate By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphate By similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
Gene namesi
Name:pdhB
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162234Add
BLAST

Proteomic databases

PRIDEiP0A0A3.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Structurei

3D structure databases

ProteinModelPortaliP0A0A3.
SMRiP0A0A3. Positions 2-325.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0022.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A0A3-1 [UniParc]FASTAAdd to Basket

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MAQMTMVQAI NDALKTELKN DQDVLIFGED VGVNGGVFRV TEGLQKEFGE    50
DRVFDTPLAE SGIGGLAMGL AVEGFRPVME VQFLGFVFEV FDAIAGQIAR 100
TRFRSGGTKT APVTIRSPFG GGVHTPELHA DNLEGILAQS PGLKVVIPSG 150
PYDAKGLLIS SIRSNDPVVY LEHMKLYRSF REEVPEEEYT IDIGKANVKK 200
EGNDISIITY GAMVQESMKA AEELEKDGYS VEVIDLRTVQ PIDVDTIVAS 250
VEKTGRAVVV QEAQRQAGVG AAVVAELSER AILSLEAPIG RVAAADTIYP 300
FTQAENVWLP NKNDIIEKAK ETLEF 325
Length:325
Mass (Da):35,246
Last modified:March 1, 2005 - v1
Checksum:i432ABDF6E4A720D5
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF235026 Genomic DNA. Translation: AAF36410.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF235026 Genomic DNA. Translation: AAF36410.1 .

3D structure databases

ProteinModelPortali P0A0A3.
SMRi P0A0A3. Positions 2-325.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P0A0A3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0022.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiODPB_STAAU
AccessioniPrimary (citable) accession number: P0A0A3
Secondary accession number(s): Q9L6H5
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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