ID KPYK_CLOPE Reviewed; 474 AA. AC Q46289; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 147. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pykF; OrderedLocusNames=CPE2149; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh- RT eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72. RC STRAIN=CPN50; RX PubMed=7559358; DOI=10.1128/jb.177.19.5680-5685.1995; RA Katayama S., Dupuy B., Garnier T., Cole S.T.; RT "Rapid expansion of the physical and genetic map of the chromosome of RT Clostridium perfringens CPN50."; RL J. Bacteriol. 177:5680-5685(1995). 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 -!- 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; BA000016; BAB81855.1; -; Genomic_DNA. DR EMBL; X86495; CAA60217.1; -; Genomic_DNA. DR RefSeq; WP_011010789.1; NC_003366.1. DR AlphaFoldDB; Q46289; -. DR SMR; Q46289; -. DR STRING; 195102.gene:10491419; -. DR KEGG; cpe:CPE2149; -. DR HOGENOM; CLU_015439_9_0_9; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000818; Chromosome. 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: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 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..474 FT /note="Pyruvate kinase" FT /id="PRO_0000112066" FT BINDING 32 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 34..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 34 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 36 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 66 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 155 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 244 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 277 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 219 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT CONFLICT 17 FT /note="E -> G (in Ref. 2; CAA60217)" FT /evidence="ECO:0000305" FT CONFLICT 45 FT /note="E -> G (in Ref. 2; CAA60217)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="E -> G (in Ref. 2; CAA60217)" FT /evidence="ECO:0000305" SQ SEQUENCE 474 AA; 52082 MW; 387970D750B2B39B CRC64; MQKTKMIFTI GPSSDSEEIL REFIRIGMNA ARLNFSHGDH ASHKEKIELI KRLRKEEKSA TAILLDIKGP KIRTYNFKNG EAELKNGDEF TFSCGDEILG DNTKCSISYK ELYEDIKPGG SILVDDGLLE FKVKEVRGTD IICEVIEGGT IKDHKGVNVP NVPIKLPAVT EKDRSDLIFG CEMEVDFVAA SFIRKPEDVL EVREILDSHG GKDIKIISKI ESQEGVDNIK EIIKVTDGVM VARGDMGVEI PIENVPIIQK NIIKKCNQAG KIVITATQML DSMIRNPRPT RAEASDVCNA IFDGTDAIML SGESASGSFP IEAAMTMSRI AKKAEANLDY NYLLRRLKDP NPNPDAFADA ISYSASKTAS KFPTKAIVAA TQTGSTAKIL SKYKPSCPII AITPYEKVRR SLALNFGIIS KKCAYFNSTD EIIEEARKVA KEFEIAETGD NIMVAAGFPT SITGGTNMLK IEKI //