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Entry: P12695
LinkDB: P12695
Original site: P12695 
ID   ODP2_YEAST              Reviewed;         482 AA.
AC   P12695; D6W1A8;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   29-OCT-2014, entry version 152.
DE   RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial;
DE            EC=2.3.1.12;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=Pyruvate dehydrogenase complex component E2;
DE            Short=PDC-E2;
DE            Short=PDCE2;
DE   Flags: Precursor;
GN   Name=LAT1; Synonyms=ODP2, PDA2; OrderedLocusNames=YNL071W;
GN   ORFNames=N2374;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-43 AND
RP   148-167, AND LIPOYLATION AT LYS-75.
RX   PubMed=3050999; DOI=10.1073/pnas.85.20.7546;
RA   Niu X.-D., Browning K.S., Behal R.H., Reed L.J.;
RT   "Cloning and nucleotide sequence of the gene for dihydrolipoamide
RT   acetyltransferase from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7546-7550(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8701611;
RX   DOI=10.1002/(SICI)1097-0061(19960330)12:4<391::AID-YEA921>3.3.CO;2-E;
RA   Poehlmann R., Philippsen P.;
RT   "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT   reveals 12 new open reading frames (ORFs) and an ancient duplication
RT   of six ORFs.";
RL   Yeast 12:391-402(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA   Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA   Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA   Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA   Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA   Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA   Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA   Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA   Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA   Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA   Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA   Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA   Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA   Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT   and its evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=7030741; DOI=10.1111/j.1432-1033.1981.tb05647.x;
RA   Kresze G.B., Ronft H.;
RT   "Pyruvate dehydrogenase complex from baker's yeast. 2. Molecular
RT   structure, dissociation, and implications for the origin of
RT   mitochondria.";
RL   Eur. J. Biochem. 119:581-587(1981).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000269|PubMed:7030741}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC   -!- COFACTOR: Binds 1 lipoyl cofactor covalently.
CC   -!- SUBUNIT: Eukaryotic pyruvate dehydrogenase (PDH) complexes are
CC       organized as a core consisting of the oligomeric dihydrolipoamide
CC       acetyl-transferase (E2), around which are arranged multiple copies
CC       of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase
CC       (E3) and protein X (E3BP) bound by non-covalent bonds.
CC       {ECO:0000269|PubMed:7030741}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: The E2 component contains covalently-bound lipoyl
CC       cofactors and it participates in the generation of acetyl groups
CC       from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to
CC       coenzyme A.
CC   -!- MISCELLANEOUS: Present with 5440 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 lipoyl-binding domain. {ECO:0000305}.
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DR   EMBL; J04096; AAA34385.1; -; Genomic_DNA.
DR   EMBL; X86470; CAA60189.1; -; Genomic_DNA.
DR   EMBL; Z71347; CAA95945.1; -; Genomic_DNA.
DR   EMBL; AY693185; AAT93204.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10474.1; -; Genomic_DNA.
DR   PIR; A30198; A30198.
DR   RefSeq; NP_014328.3; NM_001182909.3.
DR   ProteinModelPortal; P12695; -.
DR   SMR; P12695; 39-115, 173-212, 240-482.
DR   BioGrid; 35752; 158.
DR   DIP; DIP-6782N; -.
DR   IntAct; P12695; 22.
DR   MINT; MINT-650239; -.
DR   STRING; 4932.YNL071W; -.
DR   MaxQB; P12695; -.
DR   PaxDb; P12695; -.
DR   PeptideAtlas; P12695; -.
DR   EnsemblFungi; YNL071W; YNL071W; YNL071W.
DR   GeneID; 855653; -.
DR   KEGG; sce:YNL071W; -.
DR   CYGD; YNL071w; -.
DR   SGD; S000005015; LAT1.
DR   eggNOG; COG0508; -.
DR   GeneTree; ENSGT00760000119281; -.
DR   HOGENOM; HOG000281566; -.
DR   InParanoid; P12695; -.
DR   KO; K00627; -.
DR   OMA; ANEIIMP; -.
DR   OrthoDB; EOG7TTQJ2; -.
DR   BioCyc; YEAST:YNL071W-MONOMER; -.
DR   NextBio; 979905; -.
DR   PRO; PR:P12695; -.
DR   Genevestigator; P12695; -.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IDA:SGD.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IDA:SGD.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:SGD.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom.
DR   InterPro; IPR004167; E3-bd.
DR   InterPro; IPR006257; LAT1.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Complete proteome; Direct protein sequencing; Lipoyl;
KW   Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT       1     28       Mitochondrion.
FT                                {ECO:0000269|PubMed:3050999}.
FT   CHAIN        29    482       Dihydrolipoyllysine-residue
FT                                acetyltransferase component of pyruvate
FT                                dehydrogenase complex, mitochondrial.
FT                                /FTId=PRO_0000020483.
FT   DOMAIN       35    109       Lipoyl-binding.
FT   ACT_SITE    455    455       {ECO:0000255}.
FT   ACT_SITE    459    459       {ECO:0000255}.
FT   MOD_RES      75     75       N6-lipoyllysine.
FT                                {ECO:0000269|PubMed:3050999}.
SQ   SEQUENCE   482 AA;  51818 MW;  49D64C738926E784 CRC64;
     MSAFVRVVPR ISRSSVLTRS LRLQLRCYAS YPEHTIIGMP ALSPTMTQGN LAAWTKKEGD
     QLSPGEVIAE IETDKAQMDF EFQEDGYLAK ILVPEGTKDI PVNKPIAVYV EDKADVPAFK
     DFKLEDSGSD SKTSTKAQPA EPQAEKKQEA PAEETKTSAP EAKKSDVAAP QGRIFASPLA
     KTIALEKGIS LKDVHGTGPR GRITKADIES YLEKSSKQSS QTSGAAAATP AAATSSTTAG
     SAPSPSSTAS YEDVPISTMR SIIGERLLQS TQGIPSYIVS SKISISKLLK LRQSLNATAN
     DKYKLSINDL LVKAITVAAK RVPDANAYWL PNENVIRKFK NVDVSVAVAT PTGLLTPIVK
     NCEAKGLSQI SNEIKELVKR ARINKLAPEE FQGGTICISN MGMNNAVNMF TSIINPPQST
     ILAIATVERV AVEDAAAENG FSFDNQVTIT GTFDHRTIDG AKGAEFMKEL KTVIENPLEM
     LL
//
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