ID PFKA2_ASPOR Reviewed; 775 AA. AC Q9HGZ0; Q2TWS2; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 23-FEB-2022, entry version 119. DE RecName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184}; DE Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184}; DE Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184}; DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184}; DE AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184}; GN Name=pfkB; ORFNames=AO090010000444; OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. 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 Aspergillus RT 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., Kusumoto K., RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E., RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., RA Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(2005). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to CC fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03184}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. CC {ECO:0000255|HAMAP-Rule:MF_03184}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_03184}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}. 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 SMR; Q9HGZ0; -. DR STRING; 510516.Q9HGZ0; -. DR EnsemblFungi; BAE66301; BAE66301; AO090010000444. DR GeneID; 5999568; -. DR KEGG; aor:AO090010000444; -. DR VEuPathDB; FungiDB:AO090010000444; -. DR HOGENOM; CLU_011053_0_0_1; -. DR OMA; KMTGAGR; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000006564; Chromosome 8. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.460; -; 2. DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1. DR InterPro; IPR009161; 6-Pfructokinase_euk. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; ATP_PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 2. DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 2: Evidence at transcript level; KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..775 FT /note="ATP-dependent 6-phosphofructokinase 2" FT /id="PRO_0000112037" FT NP_BIND 88..89 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT NP_BIND 118..121 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 1..390 FT /note="N-terminal catalytic PFK domain 1" FT REGION 164..166 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 208..210 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 298..301 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 391..404 FT /note="Interdomain linker" FT REGION 405..775 FT /note="C-terminal regulatory PFK domain 2" FT REGION 537..541 FT /note="Fructose 2,6-bisphosphate binding; allosteric FT activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 582..584 FT /note="Fructose 2,6-bisphosphate binding; allosteric FT activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 672..675 FT /note="Fructose 2,6-bisphosphate binding; allosteric FT activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT METAL 119 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 25 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 201 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 264 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 292 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 640 FT /note="Fructose 2,6-bisphosphate; allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" 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 //