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Q89AR0

- ODP1_BUCBP

UniProt

Q89AR0 - ODP1_BUCBP

Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (16 Jun 2003)
      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

    BioCyciBAPH224915:GJ9D-189-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:bbp_189
    OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
    Taxonomic identifieri224915 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000601: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 887887Pyruvate dehydrogenase E1 componentPRO_0000162242Add
    BLAST

    Proteomic databases

    PRIDEiQ89AR0.

    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

    STRINGi224915.bbp189.

    Structurei

    3D structure databases

    ProteinModelPortaliQ89AR0.
    SMRiQ89AR0. Positions 57-887.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG2609.
    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. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000156. Pyruvate_dh_E1. 1 hit.
    SUPFAMiSSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    TIGRFAMsiTIGR00759. aceE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q89AR0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEFSSNDID PIETEDWIQA IKSVIREDGL ERANFIINTV KKYVPYKNKV    50
    VFKKCAISNY VNTIPVEEEP NYPGDLFIEQ KIRSVIRWNA IMMVLRASKK 100
    NLDLGGHLSS FQSAATIYEV CFNHFFHATN ENNGGDLVYF QGHISPGIYS 150
    RAFIEDRLTQ KQLDNFRQEI DGIGLSSYPH PKLMPNFWQF PTVSMGLGPI 200
    CAIYQAKFLK YLEHRNLKCT NNQKVYAFLG DGEMDEPESK GAISIAAREK 250
    LDNLIFIVNC NLQRLDGPVI GNGKVIDELE SVFKGCGWKV IKVIWGSKWD 300
    SLLKKDVSGK LIKLMNETLD GDYQTFKSKN GAYIRKYFFG KYLETQELVK 350
    DMSDDQIWNL DRGGHDPKKI YAALSKANSI VGKPVIILMH TVKGYGMGDI 400
    AEGKNIAHQI KKIDIKGITY IKNRFKVPVE ENELKYLPYV SFDANSIEYK 450
    YLHARRKKLG GYLPIRLSNF TNFFTLPKLD EFSTLLTEQK KEISTTIVFI 500
    RILNILLRNS FIKDRIVPII ADEARTFGME GLFRKIGIYN FIGQKYTPQD 550
    KELLAYYKED KKGQILQEGI NELGAAASWL AAATSYSTNN FPMIPFYIFY 600
    SMFGFQRIGD LFWAAGDQQA RGFLIGGTSG KTTLNGEGLQ HGDGHSHIQA 650
    LTIPNCISYN PAYAYELAVI VHDGLQRMYG PSQENIYYYI TTMNENYVMP 700
    GISKNMYEGI CKGIYKLKHV GKKNVKVQIM GSGSILQCVC RAAEILLEEY 750
    DIGSDVYSVT SFTELARNGQ DCDRWNLLHP TQEKKVPFVT KIMNKLPAIA 800
    VTDYMKLFSE QVRAYIPAVT YRVLGTDGFG RSDSRKNLRR YFEIDEYHIV 850
    IAVLGELEKI GDVDKNTIVN AISKFKIDIN KVNPRLA 887
    Length:887
    Mass (Da):100,906
    Last modified:June 16, 2003 - v1
    Checksum:i89A9A18649A6A78A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016826 Genomic DNA. Translation: AAO26921.1.
    RefSeqiNP_777816.1. NC_004545.1.

    Genome annotation databases

    EnsemblBacteriaiAAO26921; AAO26921; bbp_189.
    GeneIDi1058233.
    KEGGibab:bbp189.
    PATRICi21245153. VBIBucAph80364_0183.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016826 Genomic DNA. Translation: AAO26921.1 .
    RefSeqi NP_777816.1. NC_004545.1.

    3D structure databases

    ProteinModelPortali Q89AR0.
    SMRi Q89AR0. Positions 57-887.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224915.bbp189.

    Proteomic databases

    PRIDEi Q89AR0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO26921 ; AAO26921 ; bbp_189 .
    GeneIDi 1058233.
    KEGGi bab:bbp189.
    PATRICi 21245153. VBIBucAph80364_0183.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BAPH224915:GJ9D-189-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. 1 hit.
    [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bp.

    Entry informationi

    Entry nameiODP1_BUCBP
    AccessioniPrimary (citable) accession number: Q89AR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2003
    Last sequence update: June 16, 2003
    Last modified: October 1, 2014
    This is version 86 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