ID K6PF2_ASPOR STANDARD; PRT; 775 AA. AC Q9HGZ0; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE 6-phosphofructokinase beta subunit (EC 2.7.1.11) (Phosphofructokinase DE 2) (Phosphohexokinase) (6PF-1-K beta subunit). GN Name=pfkB; OS Aspergillus oryzae. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5062; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=RIB 40; RA Nakajima K., Kunihiro S., Sano M., Eto S., Machida M.; RT "Molecular cloning and characterization of glycolytic gene from RT Aspergillus oryzae."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. CC -!- ENZYME REGULATION: Allosterically inhibited by ATP and activated CC by AMP and fructose 2,6-bisphosphate (By similarity). CC -!- PATHWAY: Key control step of glycolysis. CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains CC subfamily. 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; AB032271; BAB12231.1; -. DR HSSP; P06998; 2PFK. DR InterPro; IPR009161; PFK_euk. DR InterPro; IPR000023; Ppfruckinase. DR Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; ATP_PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR ProDom; PD000707; Ppfruckinase; 2. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. KW Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium; KW Metal-binding; Repeat; Transferase. FT NP_BIND 35 39 ATP (By similarity). FT NP_BIND 193 197 ATP (By similarity). FT NP_BIND 210 226 ATP (By similarity). FT ACT_SITE 166 166 Proton acceptor (By similarity). FT BINDING 201 201 Substrate (By similarity). FT METAL 224 224 Magnesium (via carbonyl oxygen) (By FT similarity). FT BINDING 292 292 Substrate (By similarity). FT BINDING 298 298 Substrate (By similarity). FT BINDING 301 301 Substrate (By similarity). SQ SEQUENCE 775 AA; 84727 MW; B5A78C4F7EE43848 CRC64; MTNTILDTYS SRRKPRRIGI LTSGGDAPGM NGAIRAVVRT AIQNGCEAWA IHEGYEGLIQ GGAMMHPLYW EDVRGFLSRG GTLIGSVRCD RFREREGRLQ AARNMVLFGI DALVVCGGDG SLTGADLFRS EWPELLNELV STGVLTVAQV APHQNLNIVG LLGSIDNDFS GTDATIGCYS ALTRICEAVD AVFDTASSHR RGFVVEVMGR HCGWLALMAA IATGADWLFI PERPPRDGWE DDMCSIITKN RNRGKRRTIV ILAEGAQDSN LDRISSSAVK DVLSKRLGLD TRVTVLGHIQ RGGSPCAYDR WLSTLQGIHA VKAVLSMTPE SPSPVVIIQE NRIRTSSLAE TVALTKEANA SMHAKEFEKA ATLRDPEFME YHSAYRHLNT SDHPKMVLPE DKRMRVAIIH VGAPAAGMNP ATRAVVAYCL TRGHTPIAIH NGFPGLCRHH DDTPGSVREM HWLESGDWIN DGGSDIGTNA GLPLDDIETT AQCFERYKFD ALFVIGGFEA FTAVSQLRKA RKQYLAFRIP LVLLPASMSN NVPGTEYSLG SDTSLNTLVY FCDVVRQSAS SSGHSVFVVE AQGAEYQATA AALAAGAMTV YTPERGITLQ SLSNDIEYLR QQFSKDHGAN RSGKLIIRND QTSTIYSTTE IANIIKHEAK NRFDAQGVVP GHFQQGGKVS PIDRIRAFRL AVKCMEHLET FAGQSPEEIM NDENSATVIS IKQSRILLLP MGGPTGVEAT DTDWKRQRPK TQNWLEIQEA VDSLSGRSSL YAIPN //