ID KPYK_AGABI STANDARD; PRT; 532 AA. AC O94122; Q9UVX2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Pyruvate kinase (EC 2.7.1.40) (PK). GN Name=pkiA; OS Agaricus bisporus (Common mushroom). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes; OC Agaricales; 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; 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: ATP + pyruvate = ADP + phosphoenolpyruvate. CC -!- COFACTOR: Requires magnesium and potassium (By similarity). CC -!- PATHWAY: Glycolysis; final step. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the pyruvate kinase family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; X97579; CAA66194.1; -. DR EMBL; X91106; CAA62560.1; -. DR HSSP; P14178; 1E0T. DR InterPro; IPR011037; PK_B_barrel_like. DR InterPro; IPR001697; Pyruvate_kinase. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR ProDom; PD001009; Pyruvate_kinase; 2. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. KW Glycolysis; Kinase; Magnesium; Transferase. FT ACT_SITE 254 254 By similarity. FT METAL 256 256 Magnesium (Potential). FT METAL 277 277 Magnesium (Potential). FT METAL 278 278 Magnesium (Potential). FT BINDING 351 351 ADP (Potential). 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 //