ID KPYK_BORBU Reviewed; 477 AA. AC O51323; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=BB_0348; OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OS (Borrelia burgdorferi). OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae; OC Borreliella. OX NCBI_TaxID=224326; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."; RL Nature 390:580-586(1997). 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; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; 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; AE000783; AAC66733.1; -; Genomic_DNA. DR PIR; C70143; C70143. DR RefSeq; NP_212482.1; NC_001318.1. DR RefSeq; WP_002661716.1; NC_001318.1. DR AlphaFoldDB; O51323; -. DR SMR; O51323; -. DR STRING; 224326.BB_0348; -. DR PaxDb; 224326-BB_0348; -. DR EnsemblBacteria; AAC66733; AAC66733; BB_0348. DR KEGG; bbu:BB_0348; -. DR PATRIC; fig|224326.49.peg.744; -. DR HOGENOM; CLU_015439_0_2_12; -. DR OrthoDB; 9812123at2; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000001807; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:CAFA. 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; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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..477 FT /note="Pyruvate kinase" FT /id="PRO_0000112057" FT BINDING 34 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 36..39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 36 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 64 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 71 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 150 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 240 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 272 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 214 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 477 AA; 53032 MW; 40D3CCAC9ACB7D98 CRC64; MISKLTKIVA TISDLRCEPE HIKDLHDAGV NVIRLNTAHQ SHEDTIKVID NVRKISNKIA LMIDTKGPEV RTANIENPII VKTGDKVIIS TSPINEPNNF QTNYDGFVKE VPQGSKVLID DGELEMTVVA KLPDRLICEI KNDGQIKNKK SINTPGISLK LQSVTEKDKG FIELAAKYNV DFIAHSFVRH SKDVQDVQEI LTASGNPDVK IISKIENQEG IDNIEEIAKA SYGIMVARGD MGVEIPAEDV PIAQLKITQT CIKYGIPVIT ATQMLHTMIE NPRPTRAEVS DIANAILNGT DAIMLSGETA YGKYPIEAVK MMTSIAKKVE KHRKMTLYKD ELFYDKSITR NYIIKCAIDA TKLMDIKAII VDSLKGKTAR IMATYRASVP LFITTNSERL ARELALSYGV YSNLVDNNFK RTTEFVVTSL KMLKEQGVVN DKDTVIIISG NPNRNIEKGT EFMEINTVED AIKGRNI //