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P57301

- ODP1_BUCAI

UniProt

P57301 - ODP1_BUCAI

Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Dec 2000)
      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

    BioCyciBAPH107806:GBZJ-204-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component (EC:1.2.4.1)
    Short name:
    PDH E1 component
    Gene namesi
    Name:aceE
    Ordered Locus Names:BU205
    OrganismiBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
    Taxonomic identifieri107806 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000001806: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 887887Pyruvate dehydrogenase E1 componentPRO_0000162240Add
    BLAST

    Proteomic databases

    PRIDEiP57301.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliP57301.
    SMRiP57301. Positions 58-887.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG2609.
    HOGENOMiHOG000115215.
    KOiK00163.
    OMAiKGIYKLD.
    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.

    P57301-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSENLYNDVD PIETRDWVQA IESVIRREGH KRAHFLIEQV LKTAKINRKE    50
    FFRSSFTSDY INTISREDEY EYPGNLILEK RIRSAIRWNA IMMVLRASKK 100
    NLELGGHLSS FQSSATIYEV CFNHFFQAKN HKDGGDLVYF QGHISPGIYA 150
    RSFLEGRLSE EQIDNFRQEV DGIGLSSYPH PKLMPNFWQF PTVSMGLGPL 200
    CAIYQAKFLK YLHNRELKNT SKQIVYAFLG DGEMDEPESK GAISIAVREK 250
    LDNLIFIINC NLQRLDGPVV GNGKIVNELE SFFYGAGWKV IKVIWGSRWD 300
    CLLKKDTSGK LIQLMNETVD GDYQTFKSKD GAYVRKYFFG KYKETYDLVK 350
    DMTDEEIWKL NRGGHDPKKM FNALKKAKET KYKPTVILAH TVKGYGMGVI 400
    AEGKNIAHQI KKININGIIH IRDRFNIPVS NDEINKLPYV TFKKNSEEYC 450
    YIHSQRKKLG GYIPFRLSSF TGKLILPKLI DFQSLLEEQK KDISTTVAFI 500
    RVLNIILKNN SIKHLIVPII ADEARTFGME GLFRKIGIYS SSGQKYTPQD 550
    REQLAYYKEE KKGQILQEGI NELGAASSWL AAATSYSTND FPMILFYIYY 600
    SIFGFQRIGD LFWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS 650
    LTIPNCISYD PAFAYEVAVI IQDGLRRMYG PSQENIYYYI TTINENYYMP 700
    AMPIGVEEGI CKGIYKLKTL HGTTSKVQLI GSGAILRSVC EAAEILLKDY 750
    SITTDIYSVT SFTELARNGE DCERWNMLHP NEKNKIAYVK QIMNKNPTVA 800
    ATDYMKLFAE QIRHYIPSQE YHVLGTDGFG RSDSRDKLRD HFEVNAYYIV 850
    IAALNLLANI NDIKKKVVED AIMKFNIDAN KINPRLS 887
    Length:887
    Mass (Da):101,396
    Last modified:December 1, 2000 - v1
    Checksum:iB6AB82C012826105
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000003 Genomic DNA. Translation: BAB12922.1.
    RefSeqiNP_240036.1. NC_002528.1.

    Genome annotation databases

    EnsemblBacteriaiBAB12922; BAB12922; BAB12922.
    GeneIDi1109648.
    KEGGibuc:BU205.
    PATRICi21243928. VBIBucAph127364_0216.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000003 Genomic DNA. Translation: BAB12922.1 .
    RefSeqi NP_240036.1. NC_002528.1.

    3D structure databases

    ProteinModelPortali P57301.
    SMRi P57301. Positions 58-887.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P57301.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB12922 ; BAB12922 ; BAB12922 .
    GeneIDi 1109648.
    KEGGi buc:BU205.
    PATRICi 21243928. VBIBucAph127364_0216.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BAPH107806:GBZJ-204-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. "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
      Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
      Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: APS.

    Entry informationi

    Entry nameiODP1_BUCAI
    AccessioniPrimary (citable) accession number: P57301
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 87 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

    Documents

    1. Buchnera aphidicola (subsp. Acyrthosiphon pisum)
      Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

    External Data

    Dasty 3