ID KPYK_AGABI Reviewed; 532 AA. AC O94122; Q9UVX2; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-SEP-2023, entry version 94. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pkiA; OS Agaricus bisporus (White button mushroom). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus. OX NCBI_TaxID=5341; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Horst H39; RA Schaap P.J., Mueller Y., van Griensven L.J.L.D., Visser J.; RT "Sequence of the Agaricus bisporus pkiA gene."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE OF 3-532. RC STRAIN=Horst U1; RX AGRICOLA=IND21972038; RA De Groot P.W.J., Visser J., van Griensven L.J.L.D., Schaap P.J.; RT "Biochemical and molecular aspects of growth on fruiting of the edible RT mushroom Agaricus bisporus."; RL Mycol. Res. 102:1297-1308(1998). 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; 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 --------------------------------------------------------------------------- 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; X97579; CAA66194.1; -; Genomic_DNA. DR EMBL; X91106; CAA62560.1; -; mRNA. DR AlphaFoldDB; O94122; -. DR SMR; O94122; -. 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; 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: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. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 2: Evidence at transcript level; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Transferase. FT CHAIN 1..532 FT /note="Pyruvate kinase" FT /id="PRO_0000112106" FT BINDING 63 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 65..68 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 65 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 99 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 100 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 256 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255" FT BINDING 279 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 312 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 254 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 532 AA; 58249 MW; 3D569B9A2639CDE6 CRC64; MYPVDGIRSQ IEWNTTLNVS DAPVPTETTK YHRKTAIIAT IGPKINTVEK LTDVRLAGVN IVRMNFSHGT HEYHQSVIDN TRQMIKNDPH GRPVAIALDT KGPEIRTGQT RDGNDYPIKA GDEFIVTTDP KYSDICDNKV LFVDYANLAS VTAPGKLIYI DDGIISLLIL SIDGMNLHVR ALNNGTLSSR KGVNLPKTDV DLPPLSEKDK DDLRFGIRNG VDMIFASFIR RGEDVRQIRE VLGPDGASIK IIVKIENEQG VANFDEILKE ADGVMVARGD LGIEIPASQV FLAQKMMIAK CNIVGKPVIV ATQMLESMTY NPRPTRAEVS DVANAVLDGS DCVMLSGETA KGSYPVQSVL MMAETCLLAE TAICYPPLYD DLRAVQARPT ETAETVAIAA VAAAAEQDAK ALLVLSTSGE TARLVSKYRP KIPIITVTRN EQTARQIHLH RGCYPFWYPE PRGVQNHQWQ TDVDNRIRFG LRNALALNVI QPGASIIAVQ GWKGGLGHTN TLRILTVPTD PADLELQPLG SL //