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C6EAU2

- C6EAU2_ECOBD

UniProt

C6EAU2 - C6EAU2_ECOBD

Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Escherichia coli (strain B / BL21-DE3)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (01 Sep 2009)
      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
    2. oxidoreductase activity Source: UniProtKB-KW

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotationImported, OxidoreductaseImported, 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
    Name:aceFImported
    Ordered Locus Names:B21_00113Imported, ECBD_3504Imported, ECD_00114Imported
    OrganismiEscherichia coli (strain B / BL21-DE3)Imported
    Taxonomic identifieri469008 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001509: Chromosome, UP000002032: Chromosome, UP000009074: 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

    Protein-protein interaction databases

    STRINGi469008.ECBD_3504.

    Structurei

    3D structure databases

    ProteinModelPortaliC6EAU2.
    SMRiC6EAU2. Positions 1-81, 106-183, 206-284, 326-363, 384-630.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 3 lipoyl-binding domains.UniRule annotation

    Keywords - Domaini

    LipoylUniRule annotationSAAS annotation

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281562.
    KOiK00627.
    OMAiTEIMVAV.

    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.

    C6EAU2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ    50
    AGIVKEIKVS VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP 100
    AAAAAKDVNV PDIGSDEVEV TEILVKVGDK VEAEQSLITV EGDKASMEVP 150
    APFAGTVKEI KVNVGDKVST GSLIMVFEVA GEAGAAAPAA KQEAAPAAAP 200
    APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT VEGDKASMEV 250
    PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA 300
    AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT 350
    GRKGRILRED VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI 400
    EEVELGRIQK ISGANLSRNW VMIPHVTHFD KTDITELEAF RKQQNEEAAK 450
    RKLDVKITPV VFIMKAVAAA LEQMPRFNSS LSEDGQRLTL KKYINIGVAV 500
    DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA GEMQGGCFTI 550
    SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS 600
    FDHRVIDGAD GARFITIINN TLSDIRRLVM 630
    Length:630
    Mass (Da):66,096
    Last modified:September 1, 2009 - v1
    Checksum:i802A513A1E88F5DA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001665 Genomic DNA. Translation: ACT30503.1.
    CP001509 Genomic DNA. Translation: ACT42015.1.
    AM946981 Genomic DNA. Translation: CAQ30630.1.
    RefSeqiYP_002997980.1. NC_012892.2.
    YP_003037688.1. NC_012947.1.
    YP_003052786.1. NC_012971.2.

    Genome annotation databases

    EnsemblBacteriaiACT30503; ACT30503; ECBD_3504.
    ACT42015; ACT42015; ECD_00114.
    CAQ30630; CAQ30630; B21_00113.
    GeneIDi8115316.
    8157821.
    8181520.
    KEGGiebd:ECBD_3504.
    ebe:B21_00113.
    ebl:ECD_00114.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001665 Genomic DNA. Translation: ACT30503.1 .
    CP001509 Genomic DNA. Translation: ACT42015.1 .
    AM946981 Genomic DNA. Translation: CAQ30630.1 .
    RefSeqi YP_002997980.1. NC_012892.2.
    YP_003037688.1. NC_012947.1.
    YP_003052786.1. NC_012971.2.

    3D structure databases

    ProteinModelPortali C6EAU2.
    SMRi C6EAU2. Positions 1-81, 106-183, 206-284, 326-363, 384-630.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 469008.ECBD_3504.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACT30503 ; ACT30503 ; ECBD_3504 .
    ACT42015 ; ACT42015 ; ECD_00114 .
    CAQ30630 ; CAQ30630 ; B21_00113 .
    GeneIDi 8115316.
    8157821.
    8181520.
    KEGGi ebd:ECBD_3504.
    ebe:B21_00113.
    ebl:ECD_00114.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281562.
    KOi K00627.
    OMAi TEIMVAV.

    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. "Sequencing and gene expression analysis of Escherichia coli BL21(DE3)."
      Krempl P.M., Mairhofer J., Eisenkolb M., Specht T., Leparc G.G., Kreil D.P., Bayer K., Striedner G.
      Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BL21Imported.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B / BL21-DE3 [Austria], B / BL21-DE3 [JGI], B / BL21-DE3 [Korea]Imported and BL21Imported.
    3. "Sequencing and gene expression analysis of Escherichia coli BL21."
      Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
      Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B / BL21-DE3 [Austria]Imported.
    4. "Complete sequence of Escherichia coli 'BL21-Gold(DE3)pLysS AG'."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
      Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BL21-GoldImported.
    5. "Complete sequence of Escherichia coli BL21(DE3)."
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
      Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B / BL21-DE3 [JGI]Imported.
    6. Jeong H., Shim J.-H., Studier F.W., Oh T.K., Kim J.F.
      Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BL21.

    Entry informationi

    Entry nameiC6EAU2_ECOBD
    AccessioniPrimary (citable) accession number: C6EAU2
    Secondary accession number(s): C5W122
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 1, 2009
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 43 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