ID A0A072V223_MEDTR Unreviewed; 519 AA. AC A0A072V223; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 10-FEB-2021, entry version 37. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03186}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03186}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03186}; GN Name=25490151 {ECO:0000313|EnsemblPlants:KEH36099}; GN Synonyms=PFK {ECO:0000256|HAMAP-Rule:MF_03186}; GN OrderedLocusNames=MTR_3g110395 {ECO:0000313|EMBL:KEH36099.1}; GN ORFNames=MtrunA17_Chr3g0140611 {ECO:0000313|EMBL:RHN70911.1}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH36099.1, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:KEH36099.1, ECO:0000313|EnsemblPlants:KEH36099, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:KEH36099.1}, and cv. Jemalong A17 RC {ECO:0000313|EnsemblPlants:KEH36099, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H., RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M., RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H., RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C., RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [2] {ECO:0000313|EMBL:KEH36099.1, ECO:0000313|EnsemblPlants:KEH36099, ECO:0000313|Proteomes:UP000002051} RP GENOME REANNOTATION. RC STRAIN=A17 {ECO:0000313|EMBL:KEH36099.1}, and cv. Jemalong A17 RC {ECO:0000313|EnsemblPlants:KEH36099, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume Medicago RT truncatula."; RL BMC Genomics 15:312-312(2014). RN [3] {ECO:0000313|EnsemblPlants:KEH36099} RP IDENTIFICATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH36099}; RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. RN [4] {ECO:0000313|Proteomes:UP000265566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566}; RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7; RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S., RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M., RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W., RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F., RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F., RA Benhamed M., Crespi M., Gouzy J., Gamas P.; RT "Whole-genome landscape of Medicago truncatula symbiotic genes."; RL Nat. Plants 4:1017-1025(2018). RN [5] {ECO:0000313|EMBL:RHN70911.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaves {ECO:0000313|EMBL:RHN70911.1}; RA Pecrix Y., Gamas P., Carrere S.; RT "Whole-genome landscape of Medicago truncatula symbiotic genes."; RL Nat. Plants 0:0-0(2018). 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_03186}. 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_03186}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_03186}; CC -!- ACTIVITY REGULATION: Allosterically activated by AMP. CC {ECO:0000256|HAMAP-Rule:MF_03186}. 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_03186}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03186}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' CC sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03186}. 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; CM001219; KEH36099.1; -; Genomic_DNA. DR EMBL; PSQE01000003; RHN70911.1; -; Genomic_DNA. DR RefSeq; XP_013462064.1; XM_013606610.1. DR EnsemblPlants; KEH36099; KEH36099; MTR_3g110395. DR GeneID; 25490151; -. DR Gramene; KEH36099; KEH36099; MTR_3g110395. DR KEGG; mtr:MTR_3g110395; -. DR HOGENOM; CLU_020655_7_2_1; -. DR OrthoDB; 448001at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000002051; Chromosome 3. DR Proteomes; UP000265566; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central. 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_01981; Phosphofructokinase_II_X; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR InterPro; IPR012004; PyroP-dep_PFK_TP0108. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03186}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03186}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_03186}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03186, KW ECO:0000313|EMBL:KEH36099.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03186}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03186}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03186}; KW Reference proteome {ECO:0000313|Proteomes:UP000002051}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03186, ECO:0000313|EMBL:RHN70911.1}. FT DOMAIN 96..401 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 165..166 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT NP_BIND 190..193 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT REGION 219..221 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT REGION 264..266 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT REGION 377..380 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT REGION 470..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 237..257 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 499..519 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 221 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT METAL 191 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 102 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 320 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT SITE 192 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" SQ SEQUENCE 519 AA; 56835 MW; A1E010E9943EB73E CRC64; MASSESNSQM KVVHGDAGYI LEDVPHLSDY VPNLPTYPNP LRSNPAYSVV KQYFVHMDDT VPQKVVVHKD GPRGVHFRRA GPRQKVYFRS DDVIACIVTC GGLCPGLNTV IREIVCGLSY MYGVDKVLGI DGGYRGFYSK NTITLTPKVV NDIHKRGGTI LGTSRGGHDT GKIVDSIQDR GINQVYIIGG DGTQRGAAVI YEEVRRRGLK VAIAGIPKTI DNDIPVIDRS FGFDTAVEEA QRAINAAHVE AESVENGIGV VKLMGRYSGF IAMHATLASR DVDCCLIPES PFYLEGKGGL YEFITKRLKE SGHMVIVIAE GAGQDLLTES MQDMDQKDAS GNKLLQDVGL WISHKIKDHF AKENKMAIVL KYIDPTYMIR AIPSNASDSV YCTLLAQSAV HGAMAGYTGF TAGLVNGRHT YIPFNRITEK MNNVVITDRM WARMLSSTNQ PSFLKPKDVH QIMKAGQSPT QLLEGSNCNG GGEEAKKVEQ IPTQLMEGDK SKDNQKSRNL ADSDSCIKK //