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 16-JAN-2019, entry version 108. 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. 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 -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate CC to 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 CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, CC ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; CC Evidence={ECO:0000255|HAMAP-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 CC fructose 2,6-bisphosphate, and allosterically inhibited by ATP or CC citrate. {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) CC family. ATP-dependent PFK group I subfamily. Eukaryotic two domain CC clade "E" 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 ProteinModelPortal; Q9HGZ0; -. DR SMR; Q9HGZ0; -. DR STRING; 5062.CADAORAP00004429; -. DR EnsemblFungi; BAE66301; BAE66301; AO090010000444. DR GeneID; 5999568; -. DR KEGG; aor:AO090010000444; -. DR HOGENOM; HOG000200154; -. DR KO; K00850; -. DR OMA; PLVECVQ; -. 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 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; Complete proteome; Cytoplasm; KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 775 ATP-dependent 6-phosphofructokinase 2. FT /FTId=PRO_0000112037. FT NP_BIND 88 89 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}. FT NP_BIND 118 121 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}. FT REGION 1 390 N-terminal catalytic PFK domain 1. FT REGION 164 166 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 208 210 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 298 301 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 391 404 Interdomain linker. FT REGION 405 775 C-terminal regulatory PFK domain 2. FT REGION 537 541 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 582 584 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 672 675 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT ACT_SITE 166 166 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT METAL 119 119 Magnesium; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 25 25 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03184}. FT BINDING 201 201 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_03184}. FT BINDING 264 264 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 292 292 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_03184}. FT BINDING 640 640 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000255|HAMAP- FT 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 //