ID A0A8R2NM69_ACYPI Unreviewed; 792 AA. AC A0A8R2NM69; DT 12-OCT-2022, integrated into UniProtKB/TrEMBL. DT 12-OCT-2022, sequence version 1. DT 22-FEB-2023, entry version 3. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03184}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03184}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03184}; GN Name=100160659 {ECO:0000313|EnsemblMetazoa:XP_029343119.1}; OS Acyrthosiphon pisum (Pea aphid). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha; OC Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon. OX NCBI_TaxID=7029 {ECO:0000313|EnsemblMetazoa:XP_029343119.1, ECO:0000313|Proteomes:UP000007819}; RN [1] {ECO:0000313|Proteomes:UP000007819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819}; RA Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S., RA Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V., RA Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V., RA Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L., RA Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A., RA Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L., RA Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J., RA Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D., RA Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A., RA Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H., RA Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R., RA James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B., RA Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A., RA Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H., RA Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J., RA Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E., RA Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B., RA Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q., RA Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A., RA Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L., RA Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M., RA Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W., RA Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H., RA Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S., RA Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C., RA Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C., RA Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M., RA Weinstock G., Gibbs R.A.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:XP_029343119.1} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2022) to UniProtKB. 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP- CC Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|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:0000256|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:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_03184, CC ECO:0000256|PIRNR:PIRNR000533}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03184}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|PIRNR:PIRNR000533}. 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:0000256|HAMAP-Rule:MF_03184}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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 EnsemblMetazoa; XM_029487259.1; XP_029343119.1; LOC100160659. DR Proteomes; UP000007819; Unassembled WGS sequence. 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; 3.40.50.450; -; 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 PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE; 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 TIGRFAMs; TIGR02478; 6PF1K_euk; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03184}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03184}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_03184}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03184}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03184}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03184}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Reference proteome {ECO:0000313|Proteomes:UP000007819}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03184}. FT DOMAIN 19..324 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT DOMAIN 415..699 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 1..391 FT /note="N-terminal catalytic PFK domain 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 414..792 FT /note="C-terminal regulatory PFK domain 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT ACT_SITE 167 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 26 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 89..90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 119..122 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 120 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 165..167 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 202 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 209..211 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 265 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 293 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 299..302 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 483 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 540..544 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 578 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 585..587 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 641 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 667 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 673..676 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 748 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" SQ SEQUENCE 792 AA; 87583 MW; 10763FFF3B653A00 CRC64; MEEDQKRFIE RGSHKGKGLA VFTSGGDSQG MNAAVRAVVR MAIYLGCKVF FIKEGYQGMV DGGDNIEEAN WSSVSSIIHK GGTVIGSARC MDFKERVGRL KAACNLVKRG ITNLVVIGGD GSLTGANLFR QEWSSLLDEL LQTSQINKAE REKYKQLNIV GMVGSIDNDF CGTDMTIGTD SALHRIMDAI DAIVSTAYSH QRTFIMEVMG RHCGYLALVT ALAAEADFVF IPEWPPHQDW ASKMCKKLLQ ERTAGQRLNI IIVSEGAIDR DGQPITAEMV KQVVVDNLKQ DTRITVLGHV QRGGAPSAFD RVLGCRMGAE AVMALMEATP ETEACVVSLD GNQAVRLPLM ECVEKTKAVA KAMADKEWEL AVQLRGRSFA RNLETYKMLT RLKPPRSAFD ELGRGLSLNR EGYTLAVMHI GAPACGMNSA VRSFVRNCIY RGDTVYGIHD GVEGLVAGNI QVMQWSDVTG WVGQGGAMLG TKRTLPEKRM PEIAARLKEF NIQALLIIGG FEAYQAGIQL VQNRNNFPEF CIPMVIIPST ISNNVPGTEF SLGCDTALNE ITEICDRIRQ SAQGTKRRVF VIETMGGYCG YLATVAGLAG GADAAYIYEE KFTIKDLQND VYHMASKMAE GVQRGLILRN EKCSENYNTD FIFRLYTEEG KGLFSTRMNV LGHMQQGGSP TPFDRNMGTK QAAKCVEWLV EKLRESTRPD GTIYTDNPDT AAMMGVIRRQ YRFTPLTDLL PLTNFEQRIA KTQWWLKLRP LLRILAKHDS AYEEEGMYIT VEEGLEADTL LA //