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 01-MAY-2013, entry version 139.
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], AND PROTEIN SEQUENCE OF 29-43 AND
RP 148-167.
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 96604 / S288c / FY1679;
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;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-281, AND
RP MASS SPECTROMETRY.
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 -!- 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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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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 DIP; DIP-6782N; -.
DR IntAct; P12695; 20.
DR MINT; MINT-650239; -.
DR STRING; 4932.YNL071W; -.
DR PaxDb; P12695; -.
DR PeptideAtlas; P12695; -.
DR EnsemblFungi; YNL071W; YNL071W; YNL071W.
DR GeneID; 855653; -.
DR KEGG; sce:YNL065W; -.
DR KEGG; sce:YNL071W; -.
DR CYGD; YNL071w; -.
DR SGD; S000005015; LAT1.
DR eggNOG; COG0508; -.
DR GeneTree; ENSGT00560000077144; -.
DR HOGENOM; HOG000281566; -.
DR KO; K00627; -.
DR OMA; GTICISN; -.
DR OrthoDB; EOG4CC78S; -.
DR NextBio; 979905; -.
DR Genevestigator; P12695; -.
DR GermOnline; YNL071W; Saccharomyces cerevisiae.
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; IPR027189; LAT1_fungal.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151:SF24; PTHR23151:SF24; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; E3_bd; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 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; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1 28 Mitochondrion.
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 Potential.
FT ACT_SITE 459 459 Potential.
FT MOD_RES 75 75 N6-lipoyllysine.
FT MOD_RES 280 280 Phosphoserine.
FT MOD_RES 281 281 Phosphoserine.
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
//
