ID A0A2K1J0I5_PHYPA Unreviewed; 635 AA. AC A0A2K1J0I5; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 05-DEC-2018, entry version 7. 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 Physcomitrella patens subsp. patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR35038.1, ECO:0000313|Proteomes:UP000006727}; 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|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., Yamaguchi K., Sugano S., Kohara Y., RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., RA Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., RA Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., RA Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., RA Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., RA Sanderfoot A., Schween G., Shiu S.H., Stueber K., Theodoulou F.L., RA Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., RA Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., RA Grigoriev I.V., Quatrano R.S., Boore J.L.; RT "The Physcomitrella genome reveals evolutionary insights into the RT conquest 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|Proteomes:UP000006727}; RX PubMed=29237241; DOI=.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., RA Casacuberta J.M., Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., RA Maumus F., Salse J., Schmutz J., Rensing S.A.; RT "The Physcomitrella patens chromosome-scale assembly reveals moss RT genome structure and evolution."; RL Plant J. 93:515-533(2018). 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:0000256|HAMAP-Rule:MF_03185}. 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:456216, ChEBI:CHEBI:57634; EC=2.7.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03185}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC 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|HAMAP-Rule:MF_03185}. CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta CC (catalytic) 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) CC family. PPi-dependent PFK group II subfamily. Clade "Long" sub- CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PNR35038.1}. 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; PNR35038; PNR35038; PHYPA_022937. DR Gramene; PNR35038; PNR35038; PHYPA_022937. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000006727; Chromosome 18. 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:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro. 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_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 Complete proteome {ECO:0000313|Proteomes:UP000006727}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03185}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03185}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03185}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03185}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03185}. FT DOMAIN 104 470 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 176 177 ATP. {ECO:0000256|HAMAP-Rule:MF_03185}. FT REGION 234 236 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03185}. FT REGION 273 274 Substrate binding; shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_03185}. FT REGION 281 283 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03185}. FT REGION 448 451 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03185}. FT ACT_SITE 236 236 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03185}. FT BINDING 342 342 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03185}. FT SITE 207 207 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {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 //