ID K6PF2_ASPOR Reviewed; 775 AA. AC Q9HGZ0; Q2TWS2; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 14-DEC-2011, entry version 68. DE RecName: Full=6-phosphofructokinase subunit beta; DE EC=2.7.1.11; DE AltName: Full=6PF-1-K subunit beta; DE AltName: Full=Phosphofructokinase 2; DE AltName: Full=Phosphohexokinase; GN Name=pfkB; ORFNames=AO090010000444; OS Aspergillus oryzae (strain ATCC 42149 / RIB 40). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=510516; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 42149 / 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. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42149 / RIB 40; RX PubMed=16372010; DOI=10.1038/nature04300; RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., RA Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., RA Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., RA Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W., RA Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., RA Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., RA Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., RA Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., RA Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., RA Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., RA Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., RA Kuhara S., Ogasawara N., Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(2005). 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: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (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; -; mRNA. DR EMBL; AP007175; BAE66301.1; -; Genomic_DNA. DR RefSeq; XP_001827434.1; XM_001827382.2. DR ProteinModelPortal; Q9HGZ0; -. DR STRING; Q9HGZ0; -. DR EnsemblFungi; CADAORAT00004509; CADAORAP00004429; CADAORAG00004509. DR GeneID; 5999568; -. DR GenomeReviews; AP007175_GR; pfkB. DR KEGG; aor:AOR_1_724024; -. DR GeneTree; EFGT00050000004244; -. DR OrthoDB; EOG44N231; -. DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR InterPro; IPR009161; 6-phosphofructokinase_euk. DR InterPro; IPR022953; Phosphofructokinase. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR KO; K00850; -. DR Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; ATP_PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Ppfruckinase; 2. DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 2: Evidence at transcript level; KW Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Repeat; Transferase. FT CHAIN 1 775 6-phosphofructokinase subunit beta. FT /FTId=PRO_0000112037. 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 METAL 224 224 Magnesium; via carbonyl oxygen (By FT similarity). FT BINDING 201 201 Substrate (By 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 //