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J9YBT2

- J9YBT2_ALTMA

UniProt

J9YBT2 - J9YBT2_ALTMA

Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

MASE_14020

Organism
Alteromonas macleodii ATCC 27126
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 12 (01 Oct 2014)
      Sequence version 1 (28 Nov 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
    Gene namesi
    ORF Names:MASE_14020Imported
    OrganismiAlteromonas macleodii ATCC 27126Imported
    Taxonomic identifieri529120 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas
    ProteomesiUP000006102: 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 3 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. 3 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 3 hits.
    TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
    PS00189. LIPOYL. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    J9YBT2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDIQKIIVP DVGGDEVEVI ELCVAVGDNI EADEGVVTVE SDKASMDIPA    50
    PFEGEIVSLT VSVGDKIKEG DVIGEMKVAN GDSADKGASE ENASDESSKE 100
    DAPKQEEAPK DESKSEAAPA ASGSSEVIEV AVPDIGSDDE VDVIDVLVSV 150
    GDTIEKEDGL ITLETDKATM DVPSTHAGTV KEVFISTGDK VKEGTVVIKL 200
    EVAGSGSSSS ESASSDASSE ASAPAAQESA KQESAPAASS GSETIEVAVP 250
    DIGEDGEVDV IDVLVSAGDT VEKEDGLITL ETDKATMDVP STHAGTIKEV 300
    FIKAGDKVKQ GTLVVKLETS GGSSSSAAEK PAEAPKQEET KQDSQQEETQ 350
    QASQQEASQG RSPVPPAPEA KNTGKAHASP SVRRIAREFG VDLTQVNGSG 400
    PKNRILKEDV QAYVKAELAK PRTAAASGSA PVGDNVLQIV PVKPVDHSKF 450
    GEIEEQKLSR IQKISGPFLH RNWATIPHVT QFDEADITEV EEFRKEQNAY 500
    HAKIKSGLKI TPLVFVMKAV AKALEKYEVF NSSLSDDGES LIIKKFINIG 550
    IAVETPGGLV VPVIRDVNKK GIEQLSQELI DTSKKAREGK LKAADMQGGT 600
    FTISSLGGIG GTAFTPIVNA PEVAILGVSK SEMKPKWNGK EFEPRLMVPL 650
    SLSYDHRVID GAVGARFSTE VAANLTDLRR IIL 683
    Length:683
    Mass (Da):71,912
    Last modified:November 28, 2012 - v1
    Checksum:i67B13B76E78A3848
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003841 Genomic DNA. Translation: AFS38308.1.
    RefSeqiWP_014950395.1. NC_018632.1.
    YP_006748862.1. NC_018632.1.

    Genome annotation databases

    EnsemblBacteriaiAFS38308; AFS38308; MASE_14020.
    GeneIDi13669711.
    KEGGiamac:MASE_14020.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003841 Genomic DNA. Translation: AFS38308.1 .
    RefSeqi WP_014950395.1. NC_018632.1.
    YP_006748862.1. NC_018632.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AFS38308 ; AFS38308 ; MASE_14020 .
    GeneIDi 13669711.
    KEGGi amac:MASE_14020.

    Phylogenomic databases

    KOi K00627.

    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. 3 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 3 hits.
    TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
    PS00189. LIPOYL. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
      Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
      ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27126Imported.

    Entry informationi

    Entry nameiJ9YBT2_ALTMA
    AccessioniPrimary (citable) accession number: J9YBT2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 28, 2012
    Last sequence update: November 28, 2012
    Last modified: October 1, 2014
    This is version 12 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3