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P12695

- ODP2_YEAST

UniProt

P12695 - ODP2_YEAST

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

LAT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei455 – 4551Sequence Analysis
    Active sitei459 – 4591Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: SGD

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: SGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:YNL071W-MONOMER.

    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
    Name:LAT1
    Synonyms:ODP2, PDA2
    Ordered Locus Names:YNL071W
    ORF Names:N2374
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL071w.
    SGDiS000005015. LAT1.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrial pyruvate dehydrogenase complex Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828Mitochondrion1 PublicationAdd
    BLAST
    Chaini29 – 482454Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000020483Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751N6-lipoyllysine1 Publication

    Proteomic databases

    MaxQBiP12695.
    PaxDbiP12695.
    PeptideAtlasiP12695.

    Expressioni

    Gene expression databases

    GenevestigatoriP12695.

    Interactioni

    Subunit structurei

    Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.1 Publication

    Protein-protein interaction databases

    BioGridi35752. 158 interactions.
    DIPiDIP-6782N.
    IntActiP12695. 22 interactions.
    MINTiMINT-650239.
    STRINGi4932.YNL071W.

    Structurei

    3D structure databases

    ProteinModelPortaliP12695.
    SMRiP12695. Positions 39-115, 240-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 10975Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115591.
    HOGENOMiHOG000281566.
    KOiK00627.
    OMAiANEIIMP.
    OrthoDBiEOG7TTQJ2.

    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.

    P12695-1 [UniParc]FASTAAdd to Basket

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    MSAFVRVVPR ISRSSVLTRS LRLQLRCYAS YPEHTIIGMP ALSPTMTQGN    50
    LAAWTKKEGD QLSPGEVIAE IETDKAQMDF EFQEDGYLAK ILVPEGTKDI 100
    PVNKPIAVYV EDKADVPAFK DFKLEDSGSD SKTSTKAQPA EPQAEKKQEA 150
    PAEETKTSAP EAKKSDVAAP QGRIFASPLA KTIALEKGIS LKDVHGTGPR 200
    GRITKADIES YLEKSSKQSS QTSGAAAATP AAATSSTTAG SAPSPSSTAS 250
    YEDVPISTMR SIIGERLLQS TQGIPSYIVS SKISISKLLK LRQSLNATAN 300
    DKYKLSINDL LVKAITVAAK RVPDANAYWL PNENVIRKFK NVDVSVAVAT 350
    PTGLLTPIVK NCEAKGLSQI SNEIKELVKR ARINKLAPEE FQGGTICISN 400
    MGMNNAVNMF TSIINPPQST ILAIATVERV AVEDAAAENG FSFDNQVTIT 450
    GTFDHRTIDG AKGAEFMKEL KTVIENPLEM LL 482
    Length:482
    Mass (Da):51,818
    Last modified:October 1, 1989 - v1
    Checksum:i49D64C738926E784
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04096 Genomic DNA. Translation: AAA34385.1.
    X86470 Genomic DNA. Translation: CAA60189.1.
    Z71347 Genomic DNA. Translation: CAA95945.1.
    AY693185 Genomic DNA. Translation: AAT93204.1.
    BK006947 Genomic DNA. Translation: DAA10474.1.
    PIRiA30198.
    RefSeqiNP_014328.3. NM_001182909.3.

    Genome annotation databases

    EnsemblFungiiYNL071W; YNL071W; YNL071W.
    GeneIDi855653.
    KEGGisce:YNL071W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04096 Genomic DNA. Translation: AAA34385.1 .
    X86470 Genomic DNA. Translation: CAA60189.1 .
    Z71347 Genomic DNA. Translation: CAA95945.1 .
    AY693185 Genomic DNA. Translation: AAT93204.1 .
    BK006947 Genomic DNA. Translation: DAA10474.1 .
    PIRi A30198.
    RefSeqi NP_014328.3. NM_001182909.3.

    3D structure databases

    ProteinModelPortali P12695.
    SMRi P12695. Positions 39-115, 240-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35752. 158 interactions.
    DIPi DIP-6782N.
    IntActi P12695. 22 interactions.
    MINTi MINT-650239.
    STRINGi 4932.YNL071W.

    Proteomic databases

    MaxQBi P12695.
    PaxDbi P12695.
    PeptideAtlasi P12695.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL071W ; YNL071W ; YNL071W .
    GeneIDi 855653.
    KEGGi sce:YNL071W.

    Organism-specific databases

    CYGDi YNL071w.
    SGDi S000005015. LAT1.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115591.
    HOGENOMi HOG000281566.
    KOi K00627.
    OMAi ANEIIMP.
    OrthoDBi EOG7TTQJ2.

    Enzyme and pathway databases

    BioCyci YEAST:YNL071W-MONOMER.

    Miscellaneous databases

    NextBioi 979905.
    PROi P12695.

    Gene expression databases

    Genevestigatori P12695.

    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. "Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae."
      Niu X.-D., Browning K.S., Behal R.H., Reed L.J.
      Proc. Natl. Acad. Sci. U.S.A. 85:7546-7550(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-43 AND 148-167, LIPOYLATION AT LYS-75.
    2. "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs."
      Poehlmann R., Philippsen P.
      Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Pyruvate dehydrogenase complex from baker's yeast. 2. Molecular structure, dissociation, and implications for the origin of mitochondria."
      Kresze G.B., Ronft H.
      Eur. J. Biochem. 119:581-587(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiODP2_YEAST
    AccessioniPrimary (citable) accession number: P12695
    Secondary accession number(s): D6W1A8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
    Present with 5440 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3