ID KPYK_COREF Reviewed; 474 AA. AC Q8FP04; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 04-NOV-2026, entry version 125. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=CE1989; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). 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 -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC18799.1; Type=Erroneous initiation; Evidence={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; BA000035; BAC18799.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_006767987.1; NC_004369.1. DR AlphaFoldDB; Q8FP04; -. DR SMR; Q8FP04; -. DR STRING; 196164.gene:10742417; -. DR KEGG; cef:CE1989; -. DR eggNOG; COG0469; Bacteria. DR HOGENOM; CLU_015439_0_2_11; -. DR OMA; AAALXEI; -. DR OrthoDB; 9812123at2; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000001409; 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 FunFam; 2.40.33.10:FF:000001; Pyruvate kinase; 1. DR FunFam; 3.40.1380.20:FF:000009; Pyruvate kinase; 1. 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; NF004491; PRK05826.1; 1. DR NCBIfam; NF004886; PRK06247.1; 1. DR NCBIfam; NF004978; PRK06354.1; 1. DR NCBIfam; TIGR01064; pyruv_kin; 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. 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..474 FT /note="Pyruvate kinase" FT /id="PRO_0000112067" FT BINDING 33 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 35..38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 35 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 37 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 74 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 155 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 220 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 243 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 244 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 276 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 218 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 474 AA; 51504 MW; AC0E634D219A5BCE CRC64; MERRTKIVCT LGPAVASADG ILRLVQDGMD VARLNFSHGD HPDHEQNYKW VREATDKTGR AVGILADLQG PKIRLGRFKE GSTVWETGET VRITVDDVEG THDRVSTTYK NLAKDARPGD RLLVDDGKVG LVCVSVEGND VICEVTEGGP VSNNKGVSLP GMDISVPALS EKDIKDLRFA LKLGVDFIAL SFVRSPADVE LVHAIMDEEG RRVPVIAKLE KPEAVAALES IVLAFDAIMV ARGDLGVEVP LEEVPLVQKR AIQIARENAK PVIVATQMLD SMIENSRPTR AEASDVANAV LDGADAVMLS GETSVGKDPH NVVRTMSRIV RFAETDGRVP DLTHIPRTKR GVISYSARDI AERLNARALV AFTTSGDTAK RLARLHSHLP LLVFTPDPSV RSQLALTWGA QTFLCPKVDD TDGMMREVDR ALLAMDEYQK DDMMVVVAGS PPGVTGNTNM IHVHLLGEDT RIPK //