ID G7KHY6_MEDTR Unreviewed; 505 AA. AC G7KHY6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAR-2024, entry version 66. 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=11438579 {ECO:0000313|EnsemblPlants:AES76981}; GN Synonyms=PFK {ECO:0000256|HAMAP-Rule:MF_03186}; GN OrderedLocusNames=MTR_6g090130 {ECO:0000313|EMBL:AES76981.1}; GN ORFNames=MtrunA17_Chr6g0487421 {ECO:0000313|EMBL:RHN53070.1}; 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:AES76981.1, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:AES76981.1, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:AES76981.1}, and cv. Jemalong A17 RC {ECO:0000313|EnsemblPlants:AES76981, 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:AES76981.1, ECO:0000313|Proteomes:UP000002051} RP GENOME REANNOTATION. RC STRAIN=A17 {ECO:0000313|EMBL:AES76981.1}, and cv. Jemalong A17 RC {ECO:0000313|EnsemblPlants:AES76981, 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:AES76981} RP IDENTIFICATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES76981}; 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:RHN53070.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaves {ECO:0000313|EMBL:RHN53070.1}; 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, ECO:0000256|HAMAP- CC 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; CM001222; AES76981.1; -; Genomic_DNA. DR EMBL; PSQE01000006; RHN53070.1; -; Genomic_DNA. DR RefSeq; XP_003620763.1; XM_003620715.2. DR AlphaFoldDB; G7KHY6; -. DR STRING; 3880.G7KHY6; -. DR PaxDb; 3880-AES76981; -. DR EnsemblPlants; AES76981; AES76981; MTR_6g090130. DR GeneID; 11438579; -. DR Gramene; AES76981; AES76981; MTR_6g090130. DR KEGG; mtr:11438579; -. DR eggNOG; KOG2440; Eukaryota. DR HOGENOM; CLU_020655_7_2_1; -. DR OMA; NNRIEHK; -. DR OrthoDB; 995926at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000002051; Chromosome 6. DR Proteomes; UP000265566; Chromosome 6. 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:SF31; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1. DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 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 91..397 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 453..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 217 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 98 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 161..162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 186..189 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 187 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 215..217 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 260..262 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 316 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 373..376 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT SITE 188 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" SQ SEQUENCE 505 AA; 55211 MW; A8EDBD79C00E34E0 CRC64; MGLTEPKVVT GPAGYVLEDV PHLSDYIPDL PTYPNPLQDN PAYSVVKQYF VHVDDTVPQK VVVHKDSPRG VHFRRAGPRQ KVYFESDEIQ AAIVTCGGLC PGLNTVIREL VCSLHHMYGV TRVLGIEGGY RGFYARNTIT LTPSSVNNIH KRGGTILGTS RGGHDTNKIV DSIQDRGINQ VYIIGGDGTQ RGASVIFEEV RRRGLKCAVV GIPKTIDNDI PIIDKSFGFD TAVEEAQRAI NAAHVEAESF ENGIGVVKLM GRYSGFIAMY ATLASRDVDC CLIPESPFYL EGPGGLYEYI DRRLKENGHM VIVIAEGAGQ ELLTESLQSG KKQDASGNKL LQDVGLWISQ SIKDHFAREK TLPITLKYID PTYMIRAVPS NASDNVYCTL LAQSAVHGAM AGYTGYTSGL VNGRQTYIPF YRITERQNNV VITDRMWARL LSSTNQPSFM EVKVSDEDTK GENSLDELPD GHCSEDTSVD EITHNLGCLA PLAVPVLRTG GISGV //