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P0A0A3

- ODPB_STAAU

UniProt

P0A0A3 - ODPB_STAAU

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
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      Previous versions | rss
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    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.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 pyrophosphateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    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 betaPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    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: October 1, 2014
    This is version 42 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program