ODP2_YEAST
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 03-AUG-2022, entry version 213.
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; ORFNames=N2374;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-43 AND 148-167,
RP 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>3.0.co;2-n;
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 of six
RT 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., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT 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 structure,
RT dissociation, and implications for the origin of 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., Dephoure N.,
RA 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 phosphoproteome
RT 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:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=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 of
CC pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and
CC 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 from
CC hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme
CC A.
CC -!- MISCELLANEOUS: Present with 5440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P12695; -.
DR SMR; P12695; -.
DR BioGRID; 35752; 362.
DR ComplexPortal; CPX-3207; Mitochondrial pyruvate dehydrogenase complex.
DR DIP; DIP-6782N; -.
DR IntAct; P12695; 62.
DR MINT; P12695; -.
DR STRING; 4932.YNL071W; -.
DR iPTMnet; P12695; -.
DR SwissPalm; P12695; -.
DR MaxQB; P12695; -.
DR PaxDb; P12695; -.
DR PRIDE; P12695; -.
DR EnsemblFungi; YNL071W_mRNA; YNL071W; YNL071W.
DR GeneID; 855653; -.
DR KEGG; sce:YNL071W; -.
DR SGD; S000005015; LAT1.
DR VEuPathDB; FungiDB:YNL071W; -.
DR eggNOG; KOG0557; Eukaryota.
DR GeneTree; ENSGT00940000154943; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; P12695; -.
DR OMA; TMEFESF; -.
DR BioCyc; YEAST:YNL071W-MON; -.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SCE-70268; Pyruvate metabolism.
DR PRO; PR:P12695; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P12695; protein.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
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_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; PTHR23151; 1.
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.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Lipoyl; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:3050999"
FT CHAIN 29..482
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex, mitochondrial"
FT /id="PRO_0000020483"
FT DOMAIN 34..110
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 175..212
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 122..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 455
FT /evidence="ECO:0000255"
FT ACT_SITE 459
FT /evidence="ECO:0000255"
FT MOD_RES 75
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
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
