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G8QPQ7

- G8QPQ7_AZOSU

UniProt

G8QPQ7 - G8QPQ7_AZOSU

Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

Dsui_1577

Organism
Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma suillum)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 18 (01 Oct 2014)
      Sequence version 1 (22 Feb 2012)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.UniRule annotation

    Catalytic activityi

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.UniRule annotation
    Binds 2 lipoyl cofactors covalently.UniRule annotation
    Binds 3 lipoyl cofactors covalently.UniRule annotation

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotation, Transferase

    Keywords - Biological processi

    GlycolysisUniRule annotation

    Keywords - Ligandi

    PyruvateImported

    Enzyme and pathway databases

    BioCyciAORY640081:GHAS-1577-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
    Gene namesi
    Ordered Locus Names:Dsui_1577Imported
    OrganismiAzospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma suillum)Imported
    Taxonomic identifieri640081 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzospira
    ProteomesiUP000005633: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. pyruvate dehydrogenase complex Source: InterPro

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.UniRule annotation

    Family & Domainsi

    Sequence similaritiesi

    Contains 2 lipoyl-binding domains.UniRule annotation

    Keywords - Domaini

    LipoylUniRule annotationSAAS annotation

    Phylogenomic databases

    KOiK00627.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR006256. AcTrfase_Pyrv_DH_cplx.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    G8QPQ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTIEVKVP DIGDFKDVPV IEIFVKPGDT VKVEDPLCSL ESDKATMDVP    50
    SSAAGVVKEV KIKVGDKVAE GSVVVILESA ASGAAAAAPA PQAAAPAPVA 100
    AAPAAPAPVA AAPAPAASGP VEVKVPDIGD FKDVPVIEVF VKVGDTVKQE 150
    DALCSLESDK ATMDVPSSAA GVVKEVRVKV GDKVSEGSVV VVLEGAAGAV 200
    AAVAAAPAAA APAPAAPAVI PPELDGPAPT KPFTPAPAAA PYGLALGGKV 250
    HASPSVRAFA RELGVDLSKV TATGPKSRIQ AEDVKAYIKG VMSGQTVAPT 300
    QVGGGGITGG GSLDLLPWPK VDFAKFGPIE AKPLSRIKKI SGANLARNWV 350
    MIPAVTYHED ADITDLEAFR VQLNKENEKS GQKLTMLAFI IKACVKVLQQ 400
    FPELNTSLDG DNLVYKKYYH IGFAADTPNG LVVPVLKDAD KKGVLEIAKE 450
    TGELAKLARD GKLKPADMQG ATFTISSVGG IGGTAFSPIV NAPEVAILGV 500
    SKSSMKPVWN GKEFVPRLIV PLSLSADHRV IDGALATRFN AELAKLLADF 550
    RRVML 555
    Length:555
    Mass (Da):57,010
    Last modified:February 22, 2012 - v1
    Checksum:i37BFFFD535968CF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003153 Genomic DNA. Translation: AEV25966.1.
    RefSeqiWP_014236665.1. NC_016616.1.
    YP_005027807.1. NC_016616.1.

    Genome annotation databases

    EnsemblBacteriaiAEV25966; AEV25966; Dsui_1577.
    GeneIDi11544488.
    KEGGidsu:Dsui_1577.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003153 Genomic DNA. Translation: AEV25966.1 .
    RefSeqi WP_014236665.1. NC_016616.1.
    YP_005027807.1. NC_016616.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEV25966 ; AEV25966 ; Dsui_1577 .
    GeneIDi 11544488.
    KEGGi dsu:Dsui_1577.

    Phylogenomic databases

    KOi K00627.

    Enzyme and pathway databases

    BioCyci AORY640081:GHAS-1577-MONOMER.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR006256. AcTrfase_Pyrv_DH_cplx.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of the anaerobic perchlorate-reducing bacterium Azospira suillum strain PS."
      Byrne-Bailey K.G., Coates J.D.
      J. Bacteriol. 194:2767-2768(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-33 / DSM 13638 / PSImported.

    Entry informationi

    Entry nameiG8QPQ7_AZOSU
    AccessioniPrimary (citable) accession number: G8QPQ7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 22, 2012
    Last sequence update: February 22, 2012
    Last modified: October 1, 2014
    This is version 18 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3