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Q19749

- ODP2_CAEEL

UniProt

Q19749 - ODP2_CAEEL

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

F23B12.5

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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).Curated

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei480 – 4801Sequence Analysis
    Active sitei484 – 4841Sequence 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2
    Short name:
    PDC-E2
    Short name:
    PDCE2
    Gene namesi
    ORF Names:F23B12.5
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome V

    Organism-specific databases

    WormBaseiF23B12.5; CE09597; WBGene00009082.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. pyruvate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 507Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000244484
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei118 – 1181N6-lipoyllysineBy similarity

    Proteomic databases

    PaxDbiQ19749.

    2D gel databases

    World-2DPAGE0020:Q19749.

    Interactioni

    Protein-protein interaction databases

    BioGridi44949. 17 interactions.
    DIPiDIP-24773N.
    IntActiQ19749. 19 interactions.
    MINTiMINT-1106052.
    STRINGi6239.F23B12.5.

    Structurei

    3D structure databases

    ProteinModelPortaliQ19749.
    SMRiQ19749. Positions 80-158, 275-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 15275Lipoyl-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115591.
    HOGENOMiHOG000281566.
    InParanoidiQ19749.
    KOiK00627.
    OMAiPISNIRK.
    PhylomeDBiQ19749.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q19749-1 [UniParc]FASTAAdd to Basket

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    MSKFPVPLRT IGGLRPSTTA AISAANIGFT QSSRALSTGA AAKSSGLVGQ    50
    VARQYPNAAA FSIKQVRLYS SGNLPKHNRV ALPALSPTME LGTVVSWQKK 100
    EGDQLSEGDL LCEIETDKAT MGFETPEEGY LAKILIQEGS KDVPIGKLLC 150
    IIVDNEADVA AFKDFKDDGA SSGGSAPAAE KAPEPAKPAA SSQPSPPAQM 200
    YQAPSVPKSA PIPHSSSGRV SASPFAKKLA AENGLDLSGV SGSGPGGRIL 250
    ASDLSQAPAK GATSTTTQAV SGQDYTDIPL SNMRKTIAKR LTESKSTIPH 300
    YYLTSEIQLD TLLQVREKLN GLLAKGTSGQ ATKISINDFI IKASALACQR 350
    VPEANSYWMD SFIRENHHVD VSVAVSTPAG LITPIIFNAH AKGLATIASE 400
    IVELAQRARE GKLQPHEFQG GTFTVSNLGM FGSVSDFTAI INPPQSCILA 450
    IGGASDKLVP DEAEGYKKIK TMKVTLSCDH RTVDGAVGAV WLRHFKEFLE 500
    KPHTMLL 507
    Length:507
    Mass (Da):53,467
    Last modified:November 1, 1996 - v1
    Checksum:i2C546DA3828C5B09
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z77659 Genomic DNA. Translation: CAB01163.1.
    PIRiT21287.
    RefSeqiNP_506579.1. NM_074178.6.
    UniGeneiCel.17215.

    Genome annotation databases

    EnsemblMetazoaiF23B12.5; F23B12.5; WBGene00009082.
    GeneIDi179945.
    KEGGicel:CELE_F23B12.5.
    UCSCiF23B12.5. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z77659 Genomic DNA. Translation: CAB01163.1 .
    PIRi T21287.
    RefSeqi NP_506579.1. NM_074178.6.
    UniGenei Cel.17215.

    3D structure databases

    ProteinModelPortali Q19749.
    SMRi Q19749. Positions 80-158, 275-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 44949. 17 interactions.
    DIPi DIP-24773N.
    IntActi Q19749. 19 interactions.
    MINTi MINT-1106052.
    STRINGi 6239.F23B12.5.

    2D gel databases

    World-2DPAGE 0020:Q19749.

    Proteomic databases

    PaxDbi Q19749.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai F23B12.5 ; F23B12.5 ; WBGene00009082 .
    GeneIDi 179945.
    KEGGi cel:CELE_F23B12.5.
    UCSCi F23B12.5. c. elegans.

    Organism-specific databases

    CTDi 179945.
    WormBasei F23B12.5 ; CE09597 ; WBGene00009082 .

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115591.
    HOGENOMi HOG000281566.
    InParanoidi Q19749.
    KOi K00627.
    OMAi PISNIRK.
    PhylomeDBi Q19749.

    Miscellaneous databases

    NextBioi 907498.
    PROi Q19749.

    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 the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    2. Bienvenut W.V.
      Submitted (MAR-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 249-260; 334-350; 393-407 AND 482-493, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiODP2_CAEEL
    AccessioniPrimary (citable) accession number: Q19749
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3