PDK2_YEAST
ID PDK2_YEAST Reviewed; 491 AA.
AC P53170; D6VU82;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=[Pyruvate dehydrogenase (acetyl-transferring)] kinase 2, mitochondrial {ECO:0000305};
DE Short=PDK 2 {ECO:0000305};
DE Short=Pyruvate dehydrogenase kinase 2 {ECO:0000303|PubMed:18180296};
DE EC=2.7.11.2 {ECO:0000305|PubMed:18180296};
DE AltName: Full=Protein kinase of PDH protein 2 {ECO:0000303|PubMed:18180296};
DE AltName: Full=Pyruvate dehydrogenase complex kinase 2 {ECO:0000303|PubMed:18180296};
DE Short=PDC kinase 2 {ECO:0000303|PubMed:17918780};
DE AltName: Full=[Pyruvate dehydrogenase [lipoamide]] kinase 2 {ECO:0000303|PubMed:18180296};
DE Flags: Precursor;
GN Name=PKP2 {ECO:0000303|PubMed:18180296}; OrderedLocusNames=YGL059W;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 224-225.
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 [4]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=11152879; DOI=10.1016/s0014-5793(00)02275-4;
RA Blandin G., Durrens P., Tekaia F., Aigle M., Bolotin-Fukuhara M., Bon E.,
RA Casaregola S., de Montigny J., Gaillardin C., Lepingle A., Llorente B.,
RA Malpertuy A., Neuveglise C., Ozier-Kalogeropoulos O., Perrin A., Potier S.,
RA Souciet J.-L., Talla E., Toffano-Nioche C., Wesolowski-Louvel M., Marck C.,
RA Dujon B.;
RT "Genomic exploration of the hemiascomycetous yeasts: 4. The genome of
RT Saccharomyces cerevisiae revisited.";
RL FEBS Lett. 487:31-36(2000).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=16319894; DOI=10.1038/nature04187;
RA Ptacek J., Devgan G., Michaud G., Zhu H., Zhu X., Fasolo J., Guo H.,
RA Jona G., Breitkreutz A., Sopko R., McCartney R.R., Schmidt M.C.,
RA Rachidi N., Lee S.-J., Mah A.S., Meng L., Stark M.J.R., Stern D.F.,
RA De Virgilio C., Tyers M., Andrews B., Gerstein M., Schweitzer B.,
RA Predki P.F., Snyder M.;
RT "Global analysis of protein phosphorylation in yeast.";
RL Nature 438:679-684(2005).
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, CATALYTIC ACTIVITY, AND INTERACTION WITH
RP PKP1.
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 [10]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17918780; DOI=10.1002/yea.1543;
RA Steensma H.Y., Tomaska L., Reuven P., Nosek J., Brandt R.;
RT "Disruption of genes encoding pyruvate dehydrogenase kinases leads to
RT retarded growth on acetate and ethanol in Saccharomyces cerevisiae.";
RL Yeast 25:9-19(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. {ECO:0000269|PubMed:16319894,
CC ECO:0000269|PubMed:17918780, 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:18180296};
CC -!- SUBUNIT: Interacts with PKP1. {ECO:0000269|PubMed:18180296}.
CC -!- INTERACTION:
CC P53170; P40530: PKP1; NbExp=3; IntAct=EBI-23792, EBI-2610722;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:17918780, ECO:0000269|PubMed:18180296}.
CC -!- MISCELLANEOUS: Present with 450 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA96762.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z72581; CAA96762.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006941; DAA08043.2; -; Genomic_DNA.
DR PIR; S64063; S64063.
DR RefSeq; NP_011456.5; NM_001180924.4.
DR AlphaFoldDB; P53170; -.
DR SMR; P53170; -.
DR BioGRID; 33188; 145.
DR IntAct; P53170; 2.
DR MINT; P53170; -.
DR STRING; 4932.YGL059W; -.
DR iPTMnet; P53170; -.
DR MaxQB; P53170; -.
DR PaxDb; P53170; -.
DR PRIDE; P53170; -.
DR EnsemblFungi; YGL059W_mRNA; YGL059W; YGL059W.
DR GeneID; 852821; -.
DR KEGG; sce:YGL059W; -.
DR SGD; S000003027; PKP2.
DR VEuPathDB; FungiDB:YGL059W; -.
DR eggNOG; KOG0787; Eukaryota.
DR GeneTree; ENSGT01030000234646; -.
DR HOGENOM; CLU_023861_0_0_1; -.
DR InParanoid; P53170; -.
DR OMA; ICEAQEH; -.
DR BioCyc; YEAST:G3O-30567-MON; -.
DR PRO; PR:P53170; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53170; 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:1904183; P:negative regulation of pyruvate dehydrogenase activity; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; HDA: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; IPR036890; HATPase_C_sf.
DR PANTHER; PTHR11947; PTHR11947; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF69012; SSF69012; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Glucose metabolism; Kinase;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..491
FT /note="[Pyruvate dehydrogenase (acetyl-transferring)]
FT kinase 2, mitochondrial"
FT /id="PRO_0000202765"
FT DOMAIN 153..480
FT /note="Histidine kinase"
FT BINDING 300..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT BINDING 359..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT BINDING 383..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15119"
FT CONFLICT 224..225
FT /note="SI -> VY (in Ref. 1 and 2; CAA96762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 57294 MW; B3218D0207C47ADD CRC64;
MSKYQINCIR YRHFLRTSNI SQIPDFTKYC IGPVNEELAP YIMETMKAYP SNSEYINPQH
YYHNRTVLVE NYLKRSPNPV SLTQLAQYYD DSTKLTRTKI INSGKFVKEE LVIRIAHKLN
QLQQLPFNVV NNFHFVQVYE SYYNIFESFR KYPTIRTLED ASQFADFIKN MLEGFNTLNL
PHLIMGALEC TILDLYPREK MDQLLSDLLR ARISRRLIVE EHVSITANYT SGKEENTLVL
GDIFQECSAK KYLLEASEES QKFIQDMYFK DIPMPEFIIE GDTQLSFYFL PTHLKYLLGE
ILRNTYEATM KHYIRKGLEK PEPIIVTVVS NDESYLFRIS DKAGGVLHDD ENLWSFGKSK
ERAQESLNNF HKLPGLQTVS IYDEVHSHTK YNSKLKSLQS ITLKPYMHTS LEPMSYPSII
NGHIKYETPL IELLKRSFRY KLGIGLAMCK VYAEYWNGDL SLHSMPGYGT DVVLKLGNLM
KHTKKLQLDK V
