ID   KPYK1_CANGA             Reviewed;         501 AA.
AC   Q6FIS9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 127.
DE   RecName: Full=Pyruvate kinase 1;
DE            Short=PK 1;
DE            EC=2.7.1.40;
GN   Name=PYK1; OrderedLocusNames=CAGL0M12034g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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;
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62845.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6FIS9; -.
DR   SMR; Q6FIS9; -.
DR   FunCoup; Q6FIS9; 1050.
DR   STRING; 284593.Q6FIS9; -.
DR   EnsemblFungi; CAGL0M12034g-T; CAGL0M12034g-T-p1; CAGL0M12034g.
DR   KEGG; cgr:2891415; -.
DR   CGD; CAL0137479; PYK1.
DR   VEuPathDB; FungiDB:CAGL0M12034g; -.
DR   eggNOG; KOG2323; Eukaryota.
DR   HOGENOM; CLU_015439_0_1_1; -.
DR   InParanoid; Q6FIS9; -.
DR   OMA; RVHHIGE; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT   CHAIN           1..501
FT                   /note="Pyruvate kinase 1"
FT                   /id="PRO_0000112110"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         52..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         52
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
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         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            241
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  54668 MW;  D3F800A625D7FD4E CRC64;
     MDSRLARLTT LQTSAGEELR RTSIIGTIGP KTNNPETLVA LRKAGLNIVR MNFSHGSYEY
     HKSVIDNARK SEELYPGRPL AIALDTKGPE IRTGTTTNEV DYPIPPNHEM IFTTDDKYAK
     ACDDKIMYLD YKNITKVISA GRIIYVDDGV LSFEVLQVVD DKTLKVKSLN AGKICSHKGV
     NLPGTDVDLP ALSEKDKADL RFGVENGVHM IFASFIRTAQ DVLTIREVLG EDGKDIKIVV
     KIENQQGVNN FDEILKVTDA VMVARGDLGI EIPAPEVLAV QKKLIAKSNL AGKPVICATQ
     MLESMTYNPR PTRAEVSDVG NAVLDGADCV MLSGETAKGN YPINAVTTMA ETALIAEQAI
     AYLPNYDDIR NCTPKPTSTT ETVAASAVAA VFEQKAKAII VLSTSGTTAR LVSKYRPNCP
     IILVTRNART ARFSHLYRGV FPFVYEKESV SDWTEDVEAR LNFGIEQAIE FGILKKGDTY
     VSIQGFKAGV GHSNTLQVST A
//