ID KPYK2_CANGA Reviewed; 508 AA. AC Q6FV12; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Pyruvate kinase 2; DE Short=PK 2; DE EC=2.7.1.40; GN Name=PYK2; OrderedLocusNames=CAGL0E05610g; 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=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; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR380951; CAG58851.1; -; Genomic_DNA. DR RefSeq; XP_445932.1; XM_445932.1. DR AlphaFoldDB; Q6FV12; -. DR SMR; Q6FV12; -. DR STRING; 284593.Q6FV12; -. DR EnsemblFungi; CAGL0E05610g-T; CAGL0E05610g-T-p1; CAGL0E05610g. DR GeneID; 2887537; -. DR KEGG; cgr:CAGL0E05610g; -. DR CGD; CAL0128842; CAGL0E05610g. DR VEuPathDB; FungiDB:CAGL0E05610g; -. DR eggNOG; KOG2323; Eukaryota. DR HOGENOM; CLU_015439_0_2_1; -. DR InParanoid; Q6FV12; -. DR OMA; ESANGHY; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000002428; Chromosome E. DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD. DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi. 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; IEA:EnsemblFungi. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00288; 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; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 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..508 FT /note="Pyruvate kinase 2" FT /id="PRO_0000112111" 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 508 AA; 55598 MW; 45C66443272EC7B9 CRC64; MDSRLHRLIN LEVTPGKDVR KTAIIGTIGP KTNNVDTLVA LRKAGLNIVR MNFSHGSYEY HQSVIDNARK SEQVYPGRPL AIALDTKGPE IRTGTNVDDV DYPIPPNHEM IFTTDDKYAK ACDDKIMYVD YKNITKVIQP GKVIYVDDGV LSFEVLEVVD DKTLKVKSLN AGKISSHKGV NLPGTDVDLP ALSEKDKEDL RFGVKNGVHM IFASFIRTAQ DVLTIREVLG EEGKDIKVIV KIENQQGVNN FDEILEVAHG VMVARGDLGI EIPAPQVLAV QKKLIAKCNL AGKPVICATQ MLESMTFNPR PTRAEVSDVG NAILDGADCV MLSGETAKGN YPINAVTTMA ETAIIAERAI AYMPLYDDLR NCTPKPTSTT ETVAASAVAA VQEQGAKLIL VLSTSGNTAR LVSKYRPQCP IVLVTRNPRT ARFSHLFRGV FPFVYEKEPL DDWSEDTHAR LRFGVDMAKE YGFVKNGDAV ISIQGFKGGV GHSNTMRVSI VGGEKEDI //