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Q59097

- ODP1_CUPNH

UniProt

Q59097 - ODP1_CUPNH

Protein

Pyruvate dehydrogenase E1 component

Gene

pdhA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.By similarity

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.By 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

    Enzyme and pathway databases

    BioCyciCNEC381666:GJUJ-1371-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component (EC:1.2.4.1)
    Short name:
    PDH E1 component
    Gene namesi
    Name:pdhA
    Ordered Locus Names:H16_A1374
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 895895Pyruvate dehydrogenase E1 componentPRO_0000162238Add
    BLAST

    Proteomic databases

    PRIDEiQ59097.

    Interactioni

    Subunit structurei

    Homodimer. Part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).By similarity

    Protein-protein interaction databases

    STRINGi381666.H16_A1374.

    Structurei

    3D structure databases

    ProteinModelPortaliQ59097.
    SMRiQ59097. Positions 65-892.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG2609.
    HOGENOMiHOG000115215.
    KOiK00163.
    OMAiANMIPNC.
    OrthoDBiEOG6BW4TW.

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR004660. 2-oxoA_DH_E1.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005474. Transketolase_N.
    [Graphical view]
    PfamiPF00456. Transketolase_N. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000156. Pyruvate_dh_E1. 1 hit.
    SUPFAMiSSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    TIGRFAMsiTIGR00759. aceE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q59097-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAVPEQILG ASSANDADPQ ETHEWLDALQ GVLAAEGPAR AAFLIDKQIE    50
    YARVNGVTQP FHAETQYINT IPVEQQARIP GDQDIEHRIR SYTRWNAMAM 100
    VLRANKHTNV GGHISSFASA ATLYDVGYNH FWRAPSEAGG GDLVFVQGHS 150
    APGVYSRAFL LGRLTQDQLD NFRQEVDGKG ISSYPHPWLM PDFWQFPTVS 200
    MGLGPIMAIY QARFMKYLDS RGLAKAGDRK VWAFLGDGET DEPESLGAIG 250
    MAGREKLDNL VFVINCNLQR LDGPVRGNGK IIQELESEFR GAGWNVIKVV 300
    WGSKWDSLLA RDTKGLLMKR MMECVDGEYQ TMKAKDGAYV REHFFNTPEL 350
    KAMVADWSDD DIWRLNRGGH DPHKIYAAYK AASEHKGQPT LILAKTIKGY 400
    GMGDAGQAMN VAHQQKKMPV DAIRKFRDQF NLPVADDQLE EVPYITFPEG 450
    SKELEYMRQA RQNLGGYLPA RRQKAEALPV PQLSAFDALL KATGEGREVS 500
    TTMAFVRILN TLLKDKQIGK HVVPIVPDES RTFGMEGLFR QVGIWNQEGQ 550
    KYVPEDHDQL MFYKESQTGQ VLQEGINEAG AMCDWIAAAT SYSTHGVQMI 600
    PFYIYYSMFG IQRIGDLCWA AADMRSRGFL LGGTAGRTTL NGEGLQHEDG 650
    HSHVFHAAIP NCISYDPTFQ YELAVVMQDG LRRMYAEQED VYYYLTVMNE 700
    NYEHPEMPAG VEQDIVKGMY QFRKGVENSN APRVQLLGSG TIFREVIAAA 750
    DLLKKDWGVE SDLWGCPSFT ELAREGHDVE RFNLLHPTET PRESHVAKSL 800
    KSARGPVIAS TDYVRAFAEQ IRPFVPRRYV VLGTDGFGRS DTREKLRHFF 850
    EVDRYWVTLA ALKALADEGA IGRDKVAEAI KKYNLDPNKP NPMSV 895
    Length:895
    Mass (Da):100,365
    Last modified:November 1, 1996 - v1
    Checksum:i522A9A3C43454051
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09865 Genomic DNA. Translation: AAA21598.1.
    AM260479 Genomic DNA. Translation: CAJ92510.1.
    PIRiA55514.
    RefSeqiWP_011615027.1. NC_008313.1.
    YP_725878.1. NC_008313.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ92510; CAJ92510; H16_A1374.
    GeneIDi4250135.
    KEGGireh:H16_A1374.
    PATRICi35232211. VBIRalEut6770_1763.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09865 Genomic DNA. Translation: AAA21598.1 .
    AM260479 Genomic DNA. Translation: CAJ92510.1 .
    PIRi A55514.
    RefSeqi WP_011615027.1. NC_008313.1.
    YP_725878.1. NC_008313.1.

    3D structure databases

    ProteinModelPortali Q59097.
    SMRi Q59097. Positions 65-892.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.H16_A1374.

    Proteomic databases

    PRIDEi Q59097.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ92510 ; CAJ92510 ; H16_A1374 .
    GeneIDi 4250135.
    KEGGi reh:H16_A1374.
    PATRICi 35232211. VBIRalEut6770_1763.

    Phylogenomic databases

    eggNOGi COG2609.
    HOGENOMi HOG000115215.
    KOi K00163.
    OMAi ANMIPNC.
    OrthoDBi EOG6BW4TW.

    Enzyme and pathway databases

    BioCyci CNEC381666:GJUJ-1371-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 2 hits.
    InterProi IPR004660. 2-oxoA_DH_E1.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005474. Transketolase_N.
    [Graphical view ]
    Pfami PF00456. Transketolase_N. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000156. Pyruvate_dh_E1. 1 hit.
    SUPFAMi SSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    TIGRFAMsi TIGR00759. aceE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase."
      Hein S., Steinbuechel A.
      J. Bacteriol. 176:4394-4408(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

    Entry informationi

    Entry nameiODP1_CUPNH
    AccessioniPrimary (citable) accession number: Q59097
    Secondary accession number(s): Q0KBW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    External Data

    Dasty 3