ID A0A2K1J0I5_PHYPA Unreviewed; 635 AA. AC A0A2K1J0I5; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 29-SEP-2021, entry version 22. DE RecName: Full=Probable ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03185}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03185}; GN ORFNames=PHYPA_022937 {ECO:0000313|EMBL:PNR35038.1}; OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium. OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR35038.1}; RN [1] {ECO:0000313|EMBL:PNR35038.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c18_9850V3.1, RC ECO:0000313|Proteomes:UP000006727}; RX PubMed=18079367; DOI=10.1126/science.1150646; RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y., RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., RA Boore J.L.; RT "The Physcomitrella genome reveals evolutionary insights into the conquest RT of land by plants."; RL Science 319:64-69(2008). RN [2] {ECO:0000313|EMBL:PNR35038.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c18_9850V3.1, RC ECO:0000313|Proteomes:UP000006727}; RX PubMed=29237241; DOI=10.1111/tpj.13801; RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B., RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J., RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G., RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W., RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W., RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J., RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M., RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y., RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M., RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J., RA Schmutz J., Rensing S.A.; RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome RT structure and evolution."; RL Plant J. 93:515-533(2018). RN [3] {ECO:0000313|EnsemblPlants:Pp3c18_9850V3.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (DEC-2020) 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_03185}. 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:0000256|HAMAP- CC Rule:MF_03185}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; CC Evidence={ECO:0000256|ARBA:ARBA00000628}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_03185}; CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6- CC bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}. 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_03185}. CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic) CC chains. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily. CC {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}. 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; ABEU02000018; PNR35038.1; -; Genomic_DNA. DR EnsemblPlants; Pp3c18_9850V3.1; Pp3c18_9850V3.1; Pp3c18_9850. DR EnsemblPlants; Pp3c18_9850V3.2; Pp3c18_9850V3.2; Pp3c18_9850. DR Gramene; Pp3c18_9850V3.1; Pp3c18_9850V3.1; Pp3c18_9850. DR Gramene; Pp3c18_9850V3.2; Pp3c18_9850V3.2; Pp3c18_9850. DR OMA; NKWHCGA; -. DR OrthoDB; 1049786at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000006727; Chromosome 18. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR GO; GO:0015979; P:photosynthesis; IBA:GO_Central. DR GO; GO:0009749; P:response to glucose; IBA:GO_Central. DR Gene3D; 3.40.50.460; -; 1. DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR011183; PfpB_PPi_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR Pfam; PF00365; PFK; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. DR TIGRFAMs; TIGR02477; PFKA_PPi; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03185}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03185}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_03185}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03185}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03185}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03185}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03185}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03185}. FT DOMAIN 104..470 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 176..177 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT REGION 234..236 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT REGION 273..274 FT /note="Substrate binding; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT REGION 281..283 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT REGION 448..451 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT ACT_SITE 236 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT BINDING 342 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT SITE 207 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" SQ SEQUENCE 635 AA; 69347 MW; 4EBD12C0C3E68D69 CRC64; MGIELHRKVS KLQGLSAVRA QYQPRVPPAL KVTFAVRLAR FWGIGEVDMC GSVKVSVGDA SATAELSDRL AVSEAYPHTY GLPLVQLMSS GGPNATTAKH LPLRIGVAFC GRQSPGGHNV ITGLFDALKS QNANSILIGF IGGTEGIFSQ RTVELTNDML KDFRNQGGYD LLGRTKDQIK SYQQIKDAKA ACEALKLDVL VLIGGCGTNS DAAQLAEFFL ESGCTTKVVG IPVTIDGDLK NQFVETNVGF DTTCKVYSQL ISNICTDALS AEKYYYFIRL MGRQASHVSL ECTLQSQSNM VLLGEEVANS KMTLFDVTMQ ICDAIQARGE QGKNYGVVLL PEGLIERIPE FRALLQEINT LRKQDEDIGV DNISSRLTLW AAALYDFLPI FIKKQLLLDR ESDGSVQLSQ IETEKLLAQL VDTEMIRRTK TGLYEGKKFN AICHFFGYQA RGSLPSNFDC NYAYTLGQTA YYVAQAGLTG YMATVANLKQ DVSEWRCGGA PLTAMMSVKR WLRGPGVSQT GKPAVHTTEV DLKGKPYGLL TQHASSWLMD DLYRNPGPIQ YAGPGADLTT ITLSIEDNDY IGEIQEFYAY LDKVKEIVKP GCAGEVLKAA LSSMASVTDI LTAMSAPSYR SLTPF //