PDK1_YEAST
ID PDK1_YEAST Reviewed; 394 AA.
AC P40530; D6VVP0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=[Pyruvate dehydrogenase (acetyl-transferring)] kinase 1, mitochondrial {ECO:0000303|PubMed:16643908};
DE Short=PDK 1 {ECO:0000303|PubMed:16643908};
DE Short=Pyruvate dehydrogenase kinase 1 {ECO:0000303|PubMed:16643908};
DE EC=2.7.11.2 {ECO:0000305|PubMed:16643908, ECO:0000305|PubMed:18180296};
DE AltName: Full=Protein kinase of PDH protein 1 {ECO:0000303|PubMed:18180296};
DE AltName: Full=Pyruvate dehydrogenase complex kinase 1 {ECO:0000303|PubMed:18180296};
DE Short=PDC kinase 1 {ECO:0000303|PubMed:18180296};
DE AltName: Full=[Pyruvate dehydrogenase [lipoamide]] kinase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=PKP1 {ECO:0000303|PubMed:16643908}; OrderedLocusNames=YIL042C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=15161972; DOI=10.1073/pnas.0401263101;
RA Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C.,
RA Krauskopf A., Kupiec M., McEachern M.J.;
RT "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that
RT affect telomere length.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=16643908; DOI=10.1016/j.febslet.2006.04.002;
RA Krause-Buchholz U., Gey U., Wunschmann J., Becker S., Rodel G.;
RT "YIL042c and YOR090c encode the kinase and phosphatase of the Saccharomyces
RT cerevisiae pyruvate dehydrogenase complex.";
RL FEBS Lett. 580:2553-2560(2006).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH 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).
CC -!- FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase complex by
CC phosphorylation of the E1 alpha subunit (PDA1), thus contributing to
CC the regulation of glucose metabolism. Also involved in telomere
CC maintenance. {ECO:0000269|PubMed:15161972, ECO:0000269|PubMed:16643908,
CC ECO:0000269|PubMed:18180296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC Evidence={ECO:0000305|PubMed:16643908, ECO:0000305|PubMed:18180296};
CC -!- SUBUNIT: Interacts with PKP2. {ECO:0000269|PubMed:18180296}.
CC -!- INTERACTION:
CC P40530; P53170: PKP2; NbExp=3; IntAct=EBI-2610722, EBI-23792;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16643908,
CC ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:18180296}.
CC -!- MISCELLANEOUS: Present with 4220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000305}.
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DR EMBL; Z46861; CAA86909.1; -; Genomic_DNA.
DR EMBL; AY692706; AAT92725.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08506.1; -; Genomic_DNA.
DR PIR; S50696; S50696.
DR RefSeq; NP_012222.1; NM_001179392.1.
DR AlphaFoldDB; P40530; -.
DR SMR; P40530; -.
DR BioGRID; 34948; 82.
DR DIP; DIP-2547N; -.
DR IntAct; P40530; 5.
DR MINT; P40530; -.
DR STRING; 4932.YIL042C; -.
DR iPTMnet; P40530; -.
DR MaxQB; P40530; -.
DR PaxDb; P40530; -.
DR PRIDE; P40530; -.
DR EnsemblFungi; YIL042C_mRNA; YIL042C; YIL042C.
DR GeneID; 854769; -.
DR KEGG; sce:YIL042C; -.
DR SGD; S000001304; PKP1.
DR VEuPathDB; FungiDB:YIL042C; -.
DR eggNOG; KOG0787; Eukaryota.
DR GeneTree; ENSGT01030000234646; -.
DR HOGENOM; CLU_023861_4_1_1; -.
DR InParanoid; P40530; -.
DR OMA; IHHLALH; -.
DR BioCyc; YEAST:G3O-31314-MON; -.
DR PRO; PR:P40530; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40530; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IMP:SGD.
DR GO; GO:0015976; P:carbon utilization; IGI:SGD.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IBA:GO_Central.
DR GO; GO:1901524; P:regulation of mitophagy; IMP:SGD.
DR Gene3D; 1.20.140.20; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR11947; PTHR11947; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF69012; SSF69012; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Glucose metabolism; Kinase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..394
FT /note="[Pyruvate dehydrogenase (acetyl-transferring)]
FT kinase 1, mitochondrial"
FT /id="PRO_0000213686"
FT DOMAIN 126..386
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT BINDING 323..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT BINDING 347..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT MOD_RES 148
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 394 AA; 45444 MW; B2A996C089606961 CRC64;
MWKIMRSWKC GGMRWAHRQR PSHELLSQLS FDQHYKIRSN IELLIQDYAS KPIAPLNYEY
FLQYRPPLTK KEEYMLTIKT INLLLSLTCK RLNAIQRLPY NAVINPHIER TNSLYLKSLQ
TLLSIAYPYE LHNPPKIQAK FTELLDDHED AIVVLAKGLQ EIQSCYPKFQ ISQFLNFHLK
ERITMKLLVT HYLSLMAQNK GDTNKRMIGI LHRDLPIAQL IKHVSDYVND ICFVKFNTQR
TPVLIHPPSQ DITFTCIPPI LEYIMTEVFK NAFEAQIALG KEHMPIEINL LKPDDDELYL
RIRDHGGGIT PEVEALMFNY SYSTHTQQSA DSESTDLPGE QINNVSGMGF GLPMCKTYLE
LFGGKIDVQS LLGWGTDVYI KLKGPSKTAL LSKK
