ID   KPYK2_YEAST             Reviewed;         506 AA.
AC   P52489; D6W342;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 191.
DE   RecName: Full=Pyruvate kinase 2;
DE            Short=PK 2;
DE            EC=2.7.1.40;
GN   Name=PYK2; OrderedLocusNames=YOR347C; ORFNames=O6342;
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 90843 / S288c / FY73;
RX   PubMed=8948102;
RX   DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA   Purnelle B., Goffeau A.;
RT   "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT   chromosome XV reveals 18 open reading frames including a new pyruvate
RT   kinase and three homologues to chromosome I genes.";
RL   Yeast 12:1475-1481(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874; DOI=10.1038/387s098;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
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   [4]
RP   CHARACTERIZATION.
RX   PubMed=9139918; DOI=10.1128/jb.179.9.2987-2993.1997;
RA   Boles E., Schulte F., Miosga T., Freidel K., Schlueter E., Zimmermann F.K.,
RA   Hollenberg C.P., Heinisch J.J.;
RT   "Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in
RT   Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-
RT   bisphosphate.";
RL   J. Bacteriol. 179:2987-2993(1997).
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).
CC   -!- FUNCTION: May be used by cells under conditions in which the level of
CC       glycolytic flux is very low.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyruvate + ATP = phosphoenolpyruvate + ADP + H(+);
CC         Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=2.7.1.40;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Not activated by fructose-1,6-bisphosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 2130 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; X95720; CAA65034.1; -; Genomic_DNA.
DR   EMBL; Z75255; CAA99675.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11108.1; -; Genomic_DNA.
DR   PIR; S67256; S67256.
DR   RefSeq; NP_014992.3; NM_001183767.3.
DR   AlphaFoldDB; P52489; -.
DR   SMR; P52489; -.
DR   BioGRID; 34732; 96.
DR   FunCoup; P52489; 675.
DR   IntAct; P52489; 13.
DR   MINT; P52489; -.
DR   STRING; 4932.YOR347C; -.
DR   iPTMnet; P52489; -.
DR   PaxDb; 4932-YOR347C; -.
DR   PeptideAtlas; P52489; -.
DR   EnsemblFungi; YOR347C_mRNA; YOR347C; YOR347C.
DR   GeneID; 854529; -.
DR   KEGG; sce:YOR347C; -.
DR   AGR; SGD:S000005874; -.
DR   SGD; S000005874; PYK2.
DR   VEuPathDB; FungiDB:YOR347C; -.
DR   eggNOG; KOG2323; Eukaryota.
DR   HOGENOM; CLU_015439_0_1_1; -.
DR   InParanoid; P52489; -.
DR   OMA; FERCDES; -.
DR   OrthoDB; 108365at2759; -.
DR   BioCyc; YEAST:YOR347C-MONOMER; -.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-70171; Glycolysis.
DR   Reactome; R-SCE-70268; Pyruvate metabolism.
DR   SABIO-RK; P52489; -.
DR   UniPathway; UPA00109; UER00188.
DR   BioGRID-ORCS; 854529; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P52489; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P52489; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:1904408; F:melatonin binding; IDA:SGD.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IMP:SGD.
DR   GO; GO:0006096; P:glycolytic process; IMP:SGD.
DR   CDD; cd00288; Pyruvate_Kinase; 1.
DR   FunFam; 2.40.33.10:FF:000001; Pyruvate kinase; 1.
DR   FunFam; 3.20.20.60:FF:000025; Pyruvate kinase; 1.
DR   FunFam; 3.40.1380.20:FF:000001; Pyruvate kinase; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_kinase-like_dom_sf.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   NCBIfam; NF004491; PRK05826.1; 1.
DR   NCBIfam; NF004978; PRK06354.1; 1.
DR   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..506
FT                   /note="Pyruvate kinase 2"
FT                   /id="PRO_0000112122"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         53
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            242
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   506 AA;  55195 MW;  E0B36C298FA2E5E8 CRC64;
     MPESRLQRLA NLKIGTPQQL RRTSIIGTIG PKTNSCEAIT ALRKAGLNII RLNFSHGSYE
     FHQSVIENAV KSEQQFPGRP LAIALDTKGP EIRTGRTLND QDLYIPVDHQ MIFTTDASFA
     NTSNDKIMYI DYANLTKVIV PGRFIYVDDG ILSFKVLQII DESNLRVQAV NSGYIASHKG
     VNLPNTDVDL PPLSAKDMKD LQFGVRNGIH IVFASFIRTS EDVLSIRKAL GSEGQDIKII
     SKIENQQGLD NFDEILEVTD GVMIARGDLG IEILAPEVLA IQKKLIAKCN LAGKPVICAT
     QMLDSMTHNP RPTRAEVSDV GNAVLDGADC VMLSGETAKG DYPVNAVNIM AATALIAEST
     IAHLALYDDL RDATPKPTST TETVAAAATA AILEQDGKAI VVLSTTGNTA RLLSKYRPSC
     PIILVTRHAR TARIAHLYRG VFPFLYEPKR LDDWGEDVHR RLKFGVEMAR SFGMVDNGDT
     VVSIQGFKGG VGHSNTLRIS TVGQEF
//