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Q1RJT3

- ODP2_RICBR

UniProt

Q1RJT3 - ODP2_RICBR

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Rickettsia bellii (strain RML369-C)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (16 May 2006)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei388 – 3881Sequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Glycolysis

    Enzyme and pathway databases

    BioCyciRBEL336407:GJCY-306-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    E2
    Gene namesi
    Name:pdhC
    Ordered Locus Names:RBE_0300
    OrganismiRickettsia bellii (strain RML369-C)
    Taxonomic identifieri336407 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group
    ProteomesiUP000001951: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. pyruvate dehydrogenase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000288763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-lipoyllysineBy similarity

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

    Protein-protein interaction databases

    STRINGi336407.RBE_0300.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1RJT3.
    SMRiQ1RJT3. Positions 186-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7777Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281566.
    KOiK00627.
    OMAiGSADGQY.
    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.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q1RJT3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIKLLMPAL SPTMTEGNLA RWLKKEGDKI NPGEVIAEIE TDKATMEVEA    50
    VDEGTLAKII IPQGSQNVPV NSLIAVLIEE GEELSGIEEF IAKNNSNSPK 100
    KEEISKPAET IAPQNVKEEN ITTASDQNNI KVFASPLAKR LAKIQNVRIE 150
    EIKGSGPHGR IIKQDVLSHK GGSKALSNKI VSRNPEEYRL APNNNIRKII 200
    AKRLLESKQT VPHFYLSIEC NVDKLLDIRE DINKSFGDDK SAKISVNDFI 250
    ILAVAKALQE VPNANASWGD DAIRYYNNVD ISVAVAIENG LVTPIIRNAD 300
    QKNIVDLSSE MKGLIKKARE NKLTPEEFQG GGFTISNLGM YGIKNFNAII 350
    NPPQSCIMGV GSSSKRAIVK NDQISIATIM DVTLSADHRV VDGAVGAEFL 400
    AAFKRFIESP ALMLLYTR 418
    Length:418
    Mass (Da):45,750
    Last modified:May 16, 2006 - v1
    Checksum:iE0ECE5B73C92EC31
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000087 Genomic DNA. Translation: ABE04381.1.
    RefSeqiWP_011476992.1. NC_007940.1.
    YP_537470.1. NC_007940.1.

    Genome annotation databases

    EnsemblBacteriaiABE04381; ABE04381; RBE_0300.
    GeneIDi3996210.
    KEGGirbe:RBE_0300.
    PATRICi17881915. VBIRicBel102610_0337.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000087 Genomic DNA. Translation: ABE04381.1 .
    RefSeqi WP_011476992.1. NC_007940.1.
    YP_537470.1. NC_007940.1.

    3D structure databases

    ProteinModelPortali Q1RJT3.
    SMRi Q1RJT3. Positions 186-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 336407.RBE_0300.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE04381 ; ABE04381 ; RBE_0300 .
    GeneIDi 3996210.
    KEGGi rbe:RBE_0300.
    PATRICi 17881915. VBIRicBel102610_0337.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281566.
    KOi K00627.
    OMAi GSADGQY.
    OrthoDBi EOG610413.

    Enzyme and pathway databases

    BioCyci RBEL336407:GJCY-306-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.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
      Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
      PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RML369-C.

    Entry informationi

    Entry nameiODP2_RICBR
    AccessioniPrimary (citable) accession number: Q1RJT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 56 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

    Documents

    1. Rickettsia bellii strain RML369-C
      Rickettsia bellii (strain RML369-C): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3