ID KPYK_STAAR Reviewed; 585 AA. AC Q6GG09; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=SAR1776; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSA252; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence RT for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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; 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; BX571856; CAG40767.1; -; Genomic_DNA. DR RefSeq; WP_001232655.1; NC_002952.2. DR PDB; 3T05; X-ray; 3.05 A; A/B/C/D=1-585. DR PDB; 3T07; X-ray; 3.30 A; A/B/C/D=1-585. DR PDB; 3T0T; X-ray; 3.10 A; A/B/C/D=1-585. DR PDBsum; 3T05; -. DR PDBsum; 3T07; -. DR PDBsum; 3T0T; -. DR AlphaFoldDB; Q6GG09; -. DR SMR; Q6GG09; -. DR BindingDB; Q6GG09; -. DR ChEMBL; CHEMBL2189162; -. DR KEGG; sar:SAR1776; -. DR HOGENOM; CLU_015439_0_2_9; -. DR BRENDA; 2.7.1.40; 3352. DR UniPathway; UPA00109; UER00188. DR PRO; PR:Q6GG09; -. DR Proteomes; UP000000596; 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; 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; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Transferase. FT CHAIN 1..585 FT /note="Pyruvate kinase" FT /id="PRO_0000294130" 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" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 17..25 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 40..56 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:3T0T" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 101..107 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:3T05" FT TURN 124..127 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 128..136 FT /evidence="ECO:0007829|PDB:3T05" FT TURN 137..140 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 172..183 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 197..209 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 223..227 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 229..235 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 243..249 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 255..269 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 273..280 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:3T07" FT HELIX 291..303 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 306..310 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 312..315 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 321..336 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 340..350 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 355..370 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 373..378 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 380..382 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 383..390 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 394..402 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 404..411 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 413..420 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 427..440 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 449..454 FT /evidence="ECO:0007829|PDB:3T05" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 466..471 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 476..478 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 480..484 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 486..493 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 497..500 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 501..503 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 506..513 FT /evidence="ECO:0007829|PDB:3T05" FT TURN 517..519 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 520..523 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 526..533 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 536..538 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 539..546 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 551..553 FT /evidence="ECO:0007829|PDB:3T05" FT HELIX 558..561 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 567..571 FT /evidence="ECO:0007829|PDB:3T05" FT TURN 572..575 FT /evidence="ECO:0007829|PDB:3T05" FT STRAND 576..580 FT /evidence="ECO:0007829|PDB:3T05" SQ SEQUENCE 585 AA; 63142 MW; 87D790B356585362 CRC64; MRKTKIVCTI GPASESEEMI EKLINAGMNV ARLNFSHGSH EEHKGRIDTI RKVAKRLDKI VAILLDTKGP EIRTHNMKDG IIELERGNEV IVSMNEVEGT PEKFSVTYEN LINDVQVGSY ILLDDGLIEL QVKDIDHAKK EVKCDILNSG ELKNKKGVNL PGVRVSLPGI TEKDAEDIRF GIKENVDFIA ASFVRRPSDV LEIREILEEQ KANISVFPKI ENQEGIDNIE EILEVSDGLM VARGDMGVEI PPEKVPMVQK DLIRQCNKLG KPVITATQML DSMQRNPRAT RAEASDVANA IYDGTDAVML SGETAAGLYP EEAVKTMRNI AVSAEAAQDY KKLLSDRTKL VETSLVNAIG ISVAHTALNL NVKAIVAATE SGSTARTISK YRPHSDIIAV TPSEETARQC SIVWGVQPVV KKGRKSTDAL LNNAVATAVE TGRVTNGDLI IITAGVPTGE TGTTNMMKIH LVGDEIANGQ GIGRGSVVGT TLVAETVKDL EGKDLSDKVI VTNSIDETFV PYVEKALGLI TEENGITSPS AIVGLEKGIP TVVGVEKAVK NISNNVLVTI DAAQGKIFEG YANVL //