ID KPYK_CLOAB Reviewed; 473 AA. AC O08309; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 27-MAR-2024, entry version 140. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; Synonyms=pykA; OrderedLocusNames=CA_C0518; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 OS / VKM B-1787). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., RA Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX PubMed=9625784; DOI=10.1007/s002849900330; RA Belouski E., Watson D.E., Bennett G.N.; RT "Cloning, sequence, and expression of the phosphofructokinase gene of RT Clostridium acetobutylicum ATCC 824 in Escherichia coli."; RL Curr. Microbiol. 37:17-22(1998). 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; AE001437; AAK78498.1; -; Genomic_DNA. DR EMBL; U52366; AAB50190.1; -; Genomic_DNA. DR PIR; G96963; G96963. DR RefSeq; NP_347158.1; NC_003030.1. DR RefSeq; WP_010963840.1; NC_003030.1. DR AlphaFoldDB; O08309; -. DR SMR; O08309; -. DR STRING; 272562.CA_C0518; -. DR GeneID; 44997027; -. DR KEGG; cac:CA_C0518; -. DR PATRIC; fig|272562.8.peg.717; -. DR eggNOG; COG0469; Bacteria. DR HOGENOM; CLU_015439_0_2_9; -. DR OrthoDB; 9812123at2; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000814; 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; 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. PE 3: Inferred from homology; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. FT CHAIN 1..473 FT /note="Pyruvate kinase" FT /id="PRO_0000112064" 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 67 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" SQ SEQUENCE 473 AA; 50592 MW; 1A240576A91EEA43 CRC64; MQKTKMIFTV GPASETEEIV TAFIKAGMNA SRHNFSHGDH AEHGGRIALV KKVRAKLNKP VAICLDTKGP EIRTGDFNPS KLELQKGSKF TIVCGEEIVG DATKCSISYK DLYKDVKPGN TILIDDGLVG LTVEAIEGTN VICTVANTGL VGSHKGVNVP NVSIQLPAMT EKDKSDLIFG CKEEIDMVSA SFIRKPEDVL AIRKVLNENG GENIQIFSKI ENQEGVDNID AIIEVSDGIM VARGDMGVEI PIQRVPLIQK MIIKKCNAVG KPVITATQML DSMMRNPRPT RAEASDIANA IFDGTDAIML SGESANGSYP IEAVTTMAKI AQEAENEINY DKFLAERKGN EKKNTSDVIS LGTCTAAADL EASAIITATQ TGSTARTVSK YRPKAPVIAV TPSEKVARKL AMSWGVHPII SDKFGSTDEL ISTSVDKALE AGYVQKGDLV VVAAGVPTNV SGTTNMLKVQ VVE //