KPYK2_YEAST
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 03-AUG-2022, entry version 175.
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;
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=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
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; 90.
DR IntAct; P52489; 12.
DR MINT; P52489; -.
DR STRING; 4932.YOR347C; -.
DR iPTMnet; P52489; -.
DR MaxQB; P52489; -.
DR PaxDb; P52489; -.
DR PRIDE; P52489; -.
DR EnsemblFungi; YOR347C_mRNA; YOR347C; YOR347C.
DR GeneID; 854529; -.
DR KEGG; sce:YOR347C; -.
DR SGD; S000005874; PYK2.
DR VEuPathDB; FungiDB:YOR347C; -.
DR eggNOG; KOG2323; Eukaryota.
DR GeneTree; ENSGT00390000008859; -.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; P52489; -.
DR OMA; PGCHCAV; -.
DR BioCyc; YEAST:YOR347C-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70171; Glycolysis.
DR SABIO-RK; P52489; -.
DR UniPathway; UPA00109; UER00188.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IMP:SGD.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 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 PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 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
