ID KPYK_BACLI Reviewed; 585 AA. AC P51181; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-SEP-2023, entry version 116. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OS Bacillus licheniformis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1402; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7549104; DOI=10.1271/bbb.59.1536; RA Tanaka K., Sakai H., Ohta T., Matsuzawa H.; RT "Molecular cloning of the genes for pyruvate kinase of two bacilli, RT Bacillus psychrophilus and Bacillus licheniformis, and comparison of the RT properties of the enzymes produced in Escherichia coli."; RL Biosci. Biotechnol. Biochem. 59:1536-1542(1995). 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 -!- 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; D31955; BAA06727.1; -; Genomic_DNA. DR PIR; JC4220; JC4220. DR RefSeq; WP_009329367.1; NZ_SNWU01000003.1. DR AlphaFoldDB; P51181; -. DR SMR; P51181; -. DR PATRIC; fig|1402.63.peg.2823; -. DR OMA; RVHHIGE; -. DR BRENDA; 2.7.1.40; 669. DR UniPathway; UPA00109; UER00188. 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 CDD; cd00288; 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; 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: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. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Transferase. FT CHAIN 1..585 FT /note="Pyruvate kinase" FT /id="PRO_0000112053" 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 222 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 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 220 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 585 AA; 61943 MW; CC2A5391827D5660 CRC64; MRKTKIVCTI GPASESVEKL TQLMEAGMNV ARLNFSHGDF EEHGARIKNI REAAGKLGKD IGILLDTKGP EIRTHTMENG SIELAAGSQL IVSMDEVIGT PDKISVTYDG LIHDVSVGST ILLDDGLVGL EVTDINKDKR EIVTKVMNSG TLKNKKGVNV PGVSVNLPGI TEKDANDIVF GIEQGVDFIA ASFVRRPSDV LEIRELLEEH NAADIQIIPK IENQEGVDNI DAILEVSDGL MVARGDLGVE IPAEEVPLVQ KELIKKCNAL GKPVITATQM LDSMQRNPRP TRAEASDVAN AIFDGTDAIM LSGETAAGNY PVEAVQTMHN IASRSEEALN HKKILSARSK QVSMSITDAI GQSVAHTAIN LDVNAIVTPT ESGHTARMIS KYRPQAPIVA VTVNDAVSRK LSLVFGVFAT SGQNHSSTDE MLEKAVQKSL DTGIVRHGDL IVITAGAVGE AGTTNLMKVY VVGDVVAKGQ GIGRKSAFGE VVIAQNAQEA AKKMKDGAVL VTKSTDRDMM ASLEKAAALI TEEGGLTSHA AVVGLSLGIP VIVGMENATS ILKEGEDITV DSARGAVYKG RASVL //