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C6S7H7

- C6S7H7_NEIML

UniProt

C6S7H7 - C6S7H7_NEIML

Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Neisseria meningitidis (strain alpha14)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (22 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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotationImported, Transferase

    Keywords - Biological processi

    GlycolysisUniRule annotation

    Enzyme and pathway databases

    BioCyciNMEN662598:GJMX-1173-MONOMER.

    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:NMO_1180Imported
    OrganismiNeisseria meningitidis (strain alpha14)Imported
    Taxonomic identifieri662598 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000002054: 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

    STRINGi662598.NMO_1180.

    Structurei

    3D structure databases

    ProteinModelPortaliC6S7H7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 2 lipoyl-binding domains.UniRule annotation

    Keywords - Domaini

    LipoylUniRule annotationSAAS annotation

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281562.
    KOiK00627.
    OMAiTEIMVAV.
    OrthoDBiEOG610413.

    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.

    C6S7H7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIVEIKVPD IGGHENVDII AVEVKAGDTI AVDDTLITLE TDKATMDVPA    50
    DAAGVVKEVK VKVGDKISEG GVILTVETGA AAAEAASAAA EAQPAPAAAP 100
    VAAGGATVQV AVPDIGGHTD VDVIAVEIKV GDTVAEDDTL ITLETDKATM 150
    DVPCTAAGVV KAVFLKVGDK VSEGSAIIEV ETVGSAAAAP AQAAQAAAPA 200
    AAPPPTAAAA PAAAPAPSAP AAAKIDEAAF AKAHAGPSAR KLARELGVDL 250
    GQVKGTGLKG RIVGDDIKAF VKSVMQGGAA KPAAAGASLG SGLDLLPWPK 300
    VDFSKFGNVE VKELSRIKKI SGQNLSRNWV VIPHVTVHEE ADMTELEEFR 350
    KQLNKEWERE GVKLSPLAFI IKASVSALKA FPEFNASLDG DNLVLKNYFN 400
    IGFAADTPNG LVVPVIKDVD QKGLKQISQE LTELSKKARE GKLKPQEMQG 450
    ACFTISSLGG IGGTGFTPIV NAPEVAILGV CKSQIKPVWN GKEFAPRLMC 500
    PLSLSFDHRV IDGAAGMRFT VFLAKLLKDF RRITL 535
    Length:535
    Mass (Da):55,209
    Last modified:September 22, 2009 - v1
    Checksum:iF05F7CDA19624106
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM889136 Genomic DNA. Translation: CBA06394.1.
    RefSeqiWP_015815659.1. NC_013016.1.
    YP_003083358.1. NC_013016.1.

    Genome annotation databases

    EnsemblBacteriaiCBA06394; CBA06394; NMO_1180.
    GeneIDi8222195.
    KEGGinmi:NMO_1180.
    PATRICi20369083. VBINeiMen141067_1500.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM889136 Genomic DNA. Translation: CBA06394.1 .
    RefSeqi WP_015815659.1. NC_013016.1.
    YP_003083358.1. NC_013016.1.

    3D structure databases

    ProteinModelPortali C6S7H7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 662598.NMO_1180.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CBA06394 ; CBA06394 ; NMO_1180 .
    GeneIDi 8222195.
    KEGGi nmi:NMO_1180.
    PATRICi 20369083. VBINeiMen141067_1500.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281562.
    KOi K00627.
    OMAi TEIMVAV.
    OrthoDBi EOG610413.

    Enzyme and pathway databases

    BioCyci NMEN662598:GJMX-1173-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. "Whole-genome comparison of disease and carriage strains provides insights into virulence evolution in Neisseria meningitidis."
      Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T., Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T., Linke B., Vogel U., Frosch M.
      Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: alpha14Imported.

    Entry informationi

    Entry nameiC6S7H7_NEIML
    AccessioniPrimary (citable) accession number: C6S7H7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 22, 2009
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 36 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