ODPA_YEAST
ID ODPA_YEAST Reviewed; 420 AA.
AC P16387; D3DM87;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE EC=1.2.4.1;
DE AltName: Full=Pyruvate dehydrogenase complex component E1 alpha;
DE Short=PDHE1-A;
DE Flags: Precursor;
GN Name=PDA1; OrderedLocusNames=YER178W;
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 [MRNA], AND PROTEIN SEQUENCE OF 34-53 AND 309-322.
RX PubMed=2684159; DOI=10.1016/0006-291x(89)91549-0;
RA Behal R.H., Browning K.S., Andreed L.J.;
RT "Nucleotide and deduced amino acid sequence of the alpha subunit of yeast
RT pyruvate dehydrogenase.";
RL Biochem. Biophys. Res. Commun. 164:941-946(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=8017100; DOI=10.1002/yea.320100303;
RA Wenzel T.J., Zuurmond A.M., Bergmans A., van den Berg J.A., Steensma H.Y.;
RT "Promoter analysis of the PDA1 gene encoding the E1 alpha subunit of the
RT pyruvate dehydrogenase complex from Saccharomyces cerevisiae.";
RL Yeast 10:297-308(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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] OF 335-420.
RX PubMed=1581960; DOI=10.1016/0092-8674(92)90446-j;
RA Bishop D.K., Park D., Xu L., Kleckner N.;
RT "DMC1: a meiosis-specific yeast homolog of E. coli recA required for
RT recombination, synaptonemal complex formation, and cell cycle
RT progression.";
RL Cell 69:439-456(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-420.
RC STRAIN=SK1;
RX PubMed=8455558; DOI=10.1007/bf00282804;
RA Kobayashi T., Hotta Y., Tabata S.;
RT "Isolation and characterization of a yeast gene that is homologous with a
RT meiosis-specific cDNA from a plant.";
RL Mol. Gen. Genet. 237:225-232(1993).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [11]
RP PHOSPHORYLATION AT SER-313 BY PKP1/PKP2.
RX PubMed=18180296; DOI=10.1074/jbc.m708779200;
RA Gey U., Czupalla C., Hoflack B., Rodel G., Krause-Buchholz U.;
RT "Yeast pyruvate dehydrogenase complex is regulated by a concerted activity
RT of two kinases and two phosphatases.";
RL J. Biol. Chem. 283:9759-9767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC -!- ACTIVITY REGULATION: E1 activity is regulated by phosphorylation
CC (inactivation) and dephosphorylation (activation) of the alpha subunit.
CC -!- SUBUNIT: Pyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2
CC beta subunits. 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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Phosphorylated at Ser-313 by pyruvate dehydrogenase kinases PKP1
CC (PDK1) and PKP2 (PDK2), and dephosphorylated by pyruvate dehydrogenase
CC phosphatases PTC5 and PTC6. {ECO:0000269|PubMed:18180296}.
CC -!- MISCELLANEOUS: Present with 100000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64705.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M29582; AAA34847.1; -; mRNA.
DR EMBL; X71664; CAA50657.1; -; Genomic_DNA.
DR EMBL; U18922; AAB64705.1; ALT_INIT; Genomic_DNA.
DR EMBL; M87549; AAA34572.1; -; Genomic_DNA.
DR EMBL; D10865; BAA01636.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07841.1; -; Genomic_DNA.
DR PIR; A36743; DEBYPA.
DR RefSeq; NP_011105.4; NM_001179068.3.
DR AlphaFoldDB; P16387; -.
DR SMR; P16387; -.
DR BioGRID; 36931; 502.
DR ComplexPortal; CPX-3207; Mitochondrial pyruvate dehydrogenase complex.
DR DIP; DIP-5117N; -.
DR IntAct; P16387; 37.
DR MINT; P16387; -.
DR STRING; 4932.YER178W; -.
DR iPTMnet; P16387; -.
DR MaxQB; P16387; -.
DR PaxDb; P16387; -.
DR PRIDE; P16387; -.
DR EnsemblFungi; YER178W_mRNA; YER178W; YER178W.
DR GeneID; 856925; -.
DR KEGG; sce:YER178W; -.
DR SGD; S000000980; PDA1.
DR VEuPathDB; FungiDB:YER178W; -.
DR eggNOG; KOG0225; Eukaryota.
DR GeneTree; ENSGT00530000063174; -.
DR HOGENOM; CLU_029393_5_2_1; -.
DR InParanoid; P16387; -.
DR OMA; LGYEMPC; -.
DR BioCyc; YEAST:YER178W-MON; -.
DR BRENDA; 1.2.1.104; 984.
DR BRENDA; 1.2.4.1; 984.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SCE-70268; Pyruvate metabolism.
DR PRO; PR:P16387; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P16387; protein.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IMP:SGD.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:SGD.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR InterPro; IPR029061; THDP-binding.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Pyruvate; Reference proteome; Thiamine pyrophosphate;
KW Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2684159"
FT CHAIN 34..420
FT /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT mitochondrial"
FT /id="PRO_0000020452"
FT MOD_RES 313
FT /note="Phosphoserine; by PDK1 and PDK2"
FT /evidence="ECO:0000269|PubMed:18180296,
FT ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:17761666, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 76
FT /note="T -> S (in Ref. 1; AAA34847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46343 MW; 37019BD9E84D0002 CRC64;
MLAASFKRQP SQLVRGLGAV LRTPTRIGHV RTMATLKTTD KKAPEDIEGS DTVQIELPES
SFESYMLEPP DLSYETSKAT LLQMYKDMVI IRRMEMACDA LYKAKKIRGF CHLSVGQEAI
AVGIENAITK LDSIITSYRC HGFTFMRGAS VKAVLAELMG RRAGVSYGKG GSMHLYAPGF
YGGNGIVGAQ VPLGAGLAFA HQYKNEDACS FTLYGDGASN QGQVFESFNM AKLWNLPVVF
CCENNKYGMG TAASRSSAMT EYFKRGQYIP GLKVNGMDIL AVYQASKFAK DWCLSGKGPL
VLEYETYRYG GHSMSDPGTT YRTRDEIQHM RSKNDPIAGL KMHLIDLGIA TEAEVKAYDK
SARKYVDEQV ELADAAPPPE AKLSILFEDV YVKGTETPTL RGRIPEDTWD FKKQGFASRD
