ID KPYM_CHICK Reviewed; 530 AA. AC P00548; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 158. DE RecName: Full=Pyruvate kinase PKM; DE EC=2.7.1.40 {ECO:0000250|UniProtKB:P14618}; GN Name=PKM; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6574503; DOI=10.1073/pnas.80.12.3661; RA Lonberg N., Gilbert W.; RT "Primary structure of chicken muscle pyruvate kinase mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 80:3661-3665(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2981634; DOI=10.1016/0092-8674(85)90311-3; RA Lonberg N., Gilbert W.; RT "Intron/exon structure of the chicken pyruvate kinase gene."; RL Cell 40:81-90(1985). CC -!- FUNCTION: Glycolytic enzyme that catalyzes the transfer of a phosphoryl CC group from phosphoenolpyruvate (PEP) to ADP, generating ATP. CC {ECO:0000250|UniProtKB:P14618}. 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; Evidence={ECO:0000250|UniProtKB:P14618}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P14618}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000250|UniProtKB:P14618}; CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6- CC bisphosphate. {ECO:0000250|UniProtKB:P14618}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P14618}. CC -!- MISCELLANEOUS: This activity is regulated by glucose levels. 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; J00903; AAA49021.1; -; mRNA. DR EMBL; M18793; AAA49020.1; -; Genomic_DNA. DR EMBL; M10619; AAA49020.1; JOINED; Genomic_DNA. DR EMBL; M18788; AAA49020.1; JOINED; Genomic_DNA. DR EMBL; M18789; AAA49020.1; JOINED; Genomic_DNA. DR EMBL; M18790; AAA49020.1; JOINED; Genomic_DNA. DR EMBL; M18791; AAA49020.1; JOINED; Genomic_DNA. DR EMBL; M18792; AAA49020.1; JOINED; Genomic_DNA. DR PIR; I50408; KICHPM. DR RefSeq; NP_990800.1; NM_205469.1. DR AlphaFoldDB; P00548; -. DR SMR; P00548; -. DR BioGRID; 676705; 2. DR IntAct; P00548; 1. DR STRING; 9031.ENSGALP00000049508; -. DR PaxDb; 9031-ENSGALP00000034108; -. DR GeneID; 396456; -. DR KEGG; gga:396456; -. DR CTD; 5313; -. DR VEuPathDB; HostDB:geneid_396456; -. DR eggNOG; KOG2323; Eukaryota. DR InParanoid; P00548; -. DR OMA; RVHHIGE; -. DR PhylomeDB; P00548; -. DR Reactome; R-GGA-352882; Glycolysis. DR Reactome; R-GGA-6798695; Neutrophil degranulation. DR Reactome; R-GGA-70171; Glycolysis. DR UniPathway; UPA00109; UER00188. DR PRO; PR:P00548; -. DR Proteomes; UP000000539; Chromosome 10. DR Bgee; ENSGALG00000001992; Expressed in muscle tissue and 13 other cell types or tissues. DR ExpressionAtlas; P00548; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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:0032869; P:cellular response to insulin stimulus; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. 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; 2.40.33.10; PK beta-barrel domain-like; 1. DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 2. 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:SF101; PYRUVATE KINASE PKM; 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 2: Evidence at transcript level; KW Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P11979" FT CHAIN 2..530 FT /note="Pyruvate kinase PKM" FT /id="PRO_0000112097" FT BINDING 72 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 74..77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 74 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 76 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 112 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 113 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 206 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 269 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 271 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 294 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 295 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 431..436 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 481 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 488 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 515..520 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT SITE 269 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P00549" SQ SEQUENCE 530 AA; 58015 MW; 8B0DF09FD82EB72F CRC64; MSKHHDAGTA FIQTQQLHAA MADTFLEHMC RLDIDSEPTI ARNTGIICTI GPASRSVDKL KEMIKSGMNV ARLNFSHGTH EYHEGTIKNV REATESFASD PITYRPVAIA LDTKGPEIRT GLIKGSGTAE VELKKGAALK VTLDNAFMEN CDENVLWVDY KNLIKVIDVG SKIYVDDGLI SLLVKEKGKD FVMTEVENGG MLGSKKGVNL PGAAVDLPAV SEKDIQDLKF GVEQNVDMVF ASFIRKAADV HAVRKVLGEK GKHIKIISKI ENHEGVRRFD EIMEASDGIM VARGDLGIEI PAEKVFLAQK MMIGRCNRAG KPIICATQML ESMIKKPRPT RAEGSDVANA VLDGADCIML SGETAKGDYP LEAVRMQHAI AREAEAAMFH RQQFEEILRH SVHHREPADA MAAGAVEASF KCLAAALIVM TESGRSAHLV SRYRPRAPII AVTRNDQTAR QAHLYRGVFP VLCKQPAHDA WAEDVDLRVN LGMNVGKARG FFKTGDLVIV LTGWRPGSGY TNTMRVVPVP //