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 29-MAY-2024, entry version 127. 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; BA000056; BAE66301.1; -; Genomic_DNA. DR RefSeq; XP_001827434.1; XM_001827382.2. DR AlphaFoldDB; Q9HGZ0; -. 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; WHNLGGS; -. DR OrthoDB; 374214at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000006564; Chromosome 8. DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:TreeGrafter. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016208; F:AMP binding; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0070095; F:fructose-6-phosphate binding; IEA:TreeGrafter. DR GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048029; F:monosaccharide binding; IEA:TreeGrafter. DR GO; GO:0061621; P:canonical glycolysis; IEA:TreeGrafter. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:TreeGrafter. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.450; -; 2. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 NCBIfam; TIGR02478; 6PF1K_euk; 1. DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1. DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1. DR Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; ATP_PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 2. 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 REGION 1..390 FT /note="N-terminal catalytic PFK domain 1" FT REGION 391..404 FT /note="Interdomain linker" FT REGION 405..775 FT /note="C-terminal regulatory PFK domain 2" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 88..89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 118..121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 164..166 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 201 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 208..210 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 264 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 292 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 298..301 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 537..541 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 582..584 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 640 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 672..675 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="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 //