ID KPYK_PYRAE Reviewed; 461 AA. AC Q8ZYE0; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=PAE0819; OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP OS 104966 / NBRC 100827 / IM2). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Pyrobaculum. OX NCBI_TaxID=178306; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / RC IM2; RX PubMed=11792869; DOI=10.1073/pnas.241636498; RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., RA Miller J.H.; RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum RT aerophilum."; RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002). RN [2] RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND REGULATION. RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / RC IM2; RX PubMed=12654928; DOI=10.1074/jbc.m210288200; RA Johnsen U., Hansen T., Schoenheit P.; RT "Comparative analysis of pyruvate kinases from the hyperthermophilic RT archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum RT aerophilum and the hyperthermophilic bacterium Thermotoga maritima: unusual RT regulatory properties in hyperthermophilic archaea."; RL J. Biol. Chem. 278:25417-25427(2003). 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=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000269|PubMed:12654928}; CC -!- ACTIVITY REGULATION: Not activated by classical allosteric effectors. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=46 umol/min/mg enzyme (at 65 degrees Celsius) CC {ECO:0000269|PubMed:12654928}; CC pH dependence: CC Optimum pH is 6.0. {ECO:0000269|PubMed:12654928}; CC Temperature dependence: CC Optimum temperature is higher than 98 degrees Celsius. Thermostable CC for 2 hours up to 100 degrees Celsius. {ECO:0000269|PubMed:12654928}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12654928}. 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; AE009441; AAL63053.1; -; Genomic_DNA. DR PDB; 3QTG; X-ray; 2.20 A; A/B=1-461. DR PDBsum; 3QTG; -. DR AlphaFoldDB; Q8ZYE0; -. DR SMR; Q8ZYE0; -. DR STRING; 178306.PAE0819; -. DR EnsemblBacteria; AAL63053; AAL63053; PAE0819. DR KEGG; pai:PAE0819; -. DR PATRIC; fig|178306.9.peg.602; -. DR eggNOG; arCOG04120; Archaea. DR HOGENOM; CLU_015439_1_1_2; -. DR InParanoid; Q8ZYE0; -. DR BRENDA; 2.7.1.40; 5239. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000002439; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. FT CHAIN 1..461 FT /note="Pyruvate kinase" FT /id="PRO_0000295181" FT BINDING 46 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 48..51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 48 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 80 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 165 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 288 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 230 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT STRAND 16..22 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 25..28 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 32..39 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:3QTG" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 54..71 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 120..125 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 131..134 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 139..146 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 148..157 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 181..190 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 191..196 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 208..220 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 226..231 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 234..238 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 240..245 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 248..253 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 254..257 FT /evidence="ECO:0007829|PDB:3QTG" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:3QTG" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 266..279 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 284..291 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 302..313 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 317..321 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 323..326 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 331..343 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 358..373 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 376..380 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 385..391 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 399..404 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 406..412 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 418..422 FT /evidence="ECO:0007829|PDB:3QTG" FT HELIX 428..439 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 442..448 FT /evidence="ECO:0007829|PDB:3QTG" FT STRAND 456..460 FT /evidence="ECO:0007829|PDB:3QTG" SQ SEQUENCE 461 AA; 50262 MW; D43333DA69BDE14C CRC64; MSAPRGDHAI LRARNLTKRV ATLGPSTDVL RPDELIKFLD LVDGVRINLA HASPNEVKFR IEAVRSYEKA KNRPLAVIVD LKGPSIRVGS TSPINVQEGE VVKFKLSDKS DGTYIPVPNK AFFSAVEQND VILMLDGRLR LKVTNTGSDW IEAVAESSGV ITGGKAIVVE GKDYDISTPA EEDVEALKAI SPIRDNIDYV AISLAKSCKD VDSVRSLLTE LGFQSQVAVK IETKGAVNNL EELVQCSDYV VVARGDLGLH YGLDALPIVQ RRIVHTSLKY GKPIAVATQL LDSMQSSPIP TRAEINDVFT TASMGVDSLW LTNETASGKY PLAAVSWLSR ILMNVEYQIP QSPLLQNSRD RFAKGLVELA QDLGANILVF SMSGTLARRI AKFRPRGVVY VGTPNVRVAR SLSIVWALEP LYIPAENYEE GLEKLISLKG TTPFVATYGI RGGVHSVKVK L //