ID KPYK_STAA3 Reviewed; 585 AA. AC Q2FG40; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 106. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=SAUSA300_1644; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). 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; 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 -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing CC enzyme 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; CP000255; ABD22512.1; -; Genomic_DNA. DR RefSeq; WP_001232648.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FG40; -. DR SMR; Q2FG40; -. DR KEGG; saa:SAUSA300_1644; -. DR HOGENOM; CLU_015439_0_2_9; -. DR OMA; RVHHIGE; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000001939; Chromosome. 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:0006950; P:response to stress; IEA:UniProtKB-ARBA. DR FunFam; 2.40.33.10:FF:000001; Pyruvate kinase; 1. DR FunFam; 3.20.20.60:FF:000001; Pyruvate kinase; 1. DR FunFam; 3.40.1380.20:FF:000017; Pyruvate kinase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 3.50.30.10; Phosphohistidine domain; 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; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR036637; Phosphohistidine_dom_sf. 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; NF004491; PRK05826.1; 1. DR NCBIfam; NF004978; PRK06354.1; 1. DR NCBIfam; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817; PYRUVATE KINASE; 1. DR Pfam; PF00391; PEP-utilizers; 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; SSF52009; Phosphohistidine 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..585 FT /note="Pyruvate kinase" FT /id="PRO_0000294136" 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 156 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 585 AA; 63102 MW; 4AB45FDE55BF577D CRC64; MRKTKIVCTI GPASESEEMI EKLINAGMNV ARLNFSHGSH EEHKGRIDTI RKVAKRLDKI VAILLDTKGP EIRTHNMKDG IIELERGNEV IVSMNEVEGT PEKFSVTYEN LINDVQVGSY ILLDDGLIEL QVKDIDHAKK EVKCDILNSG ELKNKKGVNL PGVRVSLPGI TEKDAEDIRF GIKENVDFIA ASFVRRPSDV LEIREILEEQ KANISVFPKI ENQEGIDNIA EILEVSDGLM VARGDMGVEI PPEKVPMVQK DLIRQCNKLG KPVITATQML DSMQRNPRAT RAEASDVANA IYDGTDAVML SGETAAGLYP EEAVKTMRNI AVSAEAAQDY KKLLSDRTKL VETSLVNAIG ISVAHTALNL NVKAIVAATE SGSTARTISK YRPHSDIIAV TPSEETARQC SIVWGVQPVV KKGRKSTDAL LNNAVATAVE TGRVSNGDLI IITAGVPTGE TGTTNMMKIH LVGDEIANGQ GIGRGSVVGT TLVAETVKDL EGKDLSDKVI VTNSIDETFV PYVEKALGLI TEENGITSPS AIVGLEKGIP TVVGVEKAVK NISNNMLVTI DAAQGKIFEG YANVL //