ID A0A072V223_MEDTR Unreviewed; 519 AA. AC A0A072V223; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 29-MAY-2024, entry version 51. 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|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., Geurts R., Cannon S.B., Udvardi M.K., RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., RA 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|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|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|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 AlphaFoldDB; A0A072V223; -. DR STRING; 3880.A0A072V223; -. DR EnsemblPlants; KEH36099; KEH36099; MTR_3g110395. DR GeneID; 25490151; -. DR Gramene; KEH36099; KEH36099; MTR_3g110395. DR KEGG; mtr:25490151; -. DR HOGENOM; CLU_020655_7_2_1; -. DR OrthoDB; 995926at2759; -. 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 Gene3D; 3.40.50.450; -; 1. 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 PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1. DR PANTHER; PTHR45770:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 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 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 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}. FT DOMAIN 96..401 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 470..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 499..519 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 221 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 165..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 190..193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 219..221 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 264..266 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 320 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 377..380 FT /ligand="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 //