ID KPYK_EMENI STANDARD; PRT; 526 AA. AC P22360; DT 01-AUG-1991 (REL. 19, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE PYRUVATE KINASE (EC 2.7.1.40) (PK). GN PKIA OR PKI. OS EMERICELLA NIDULANS (ASPERGILLUS NIDULANS). OC EUKARYOTA; FUNGI; ASCOMYCOTA; EUASCOMYCETES; PLECTOMYCETES; OC EUROTIALES; TRICHOCOMACEAE; EMERICELLA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WG096; RX MEDLINE; 89208879. RA DE GRAAFF L., VISSER J.; RT "Structure of the Aspergillus nidulans pyruvate kinase gene."; RL CURR. GENET. 14:553-560(1988). CC -!- CATALYTIC ACTIVITY: ATP + PYRUVATE = ADP + PHOSPHOENOLPYRUVATE. CC -!- COFACTOR: REQUIRES MAGNESIUM AND POTASSIUM. CC -!- ENZYME REGULATION: REGULATED BY PHOSPHOENOLPYRUVATE SUBSTRATE AND CC ALLOSTERIC EFFECTORS SUCH AS FRUCTOSE 1,6 DIPHOSPHATE AND CC MAGNESIUM. CC -!- PATHWAY: FINAL STEP IN GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. 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 by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; M36918; G168074; -. DR PIR; S27364; S27364. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. DR PFAM; PF00224; PK; 1. DR HSSP; P00549; 1A3W. KW TRANSFERASE; KINASE; GLYCOLYSIS; MAGNESIUM; PHOSPHORYLATION. FT MOD_RES 36 36 PHOSPHORYLATION (POTENTIAL). 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 526 AA; 58075 MW; 771B65CF CRC32; MAASSSLDHL SNRMKLEWHS KLNTEMVPAK NFRRTSIICT IGPKTNSVEK INALRRAGLN VVRMNFSHGS YEYHQSVIDH AREAEKQAAG RPVAIALDTK GPEIRTGNTV GDKDIPIKAG HEMNISTDEQ YATASDDQNM YVDYKNITKV ISAGKLIYVD DGILSFEVLE VVDDKTLRVR CLNNGNISSR KGVNLPGTDV DLPALSEKDI SDLKFGVKNK VDMVFASFIR RGSDIRHIRE VLGEEGREIQ IIAKIENQQG VNNFDEILEE TDGVMVARGD LGIEIPAPKV FIAQKMMIAK CNIKGKPVIC ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA KGNYPCEAVT MMSETCLLAE VAIPHFNVFD ELRNLAPRPT DTVESIAMAA VSASLELNAG AIVVLTTSGN TARMISKYRP VCPIIMVSRN PAATRYSHLY RGVWPFYFPE KKPDFNVKIW QEDVDRRLKW GINHGLKLGI INKGDNIVCV QGWRGGMGHT NTVRVVPAEE NLGLSE //