ID C5YAA9_SORBI Unreviewed; 484 AA. AC C5YAA9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 74. 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=PFK {ECO:0000256|HAMAP-Rule:MF_03186}; GN ORFNames=SORBI_3006G114700 {ECO:0000313|EMBL:EES12338.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EES12338.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EES12338.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). RN [2] {ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=29161754; DOI=10.1111/tpj.13781; RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D., RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A., RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.; RT "The Sorghum bicolor reference genome: improved assembly, gene annotations, RT a transcriptome atlas, and signatures of genome organization."; RL Plant J. 93:338-354(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; CM000765; EES12338.1; -; Genomic_DNA. DR RefSeq; XP_002448010.1; XM_002447965.1. DR AlphaFoldDB; C5YAA9; -. DR STRING; 4558.C5YAA9; -. DR EnsemblPlants; EES12338; EES12338; SORBI_3006G114700. DR GeneID; 8073561; -. DR Gramene; EES12338; EES12338; SORBI_3006G114700. DR KEGG; sbi:8073561; -. DR eggNOG; KOG2440; Eukaryota. DR HOGENOM; CLU_020655_7_3_1; -. DR InParanoid; C5YAA9; -. DR OMA; IGIRRGW; -. DR OrthoDB; 995926at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000768; 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; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1. DR PANTHER; PTHR45770:SF9; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 2; 1. DR Pfam; PF00365; PFK; 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:UP000000768}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03186}. FT DOMAIN 118..427 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..32 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 246 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 125 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 190..191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 215..218 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 244..246 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 289..291 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 345 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 403..406 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT SITE 217 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" SQ SEQUENCE 484 AA; 51972 MW; 078F61B4B948AC1F CRC64; MDPTAARSSG GTPAAAENDA TAPTNTTVTL PPLTLRDVPR LPSALASAAS PSPTPAVQNP ISRHPYFHPP ATFYISPGDV TLRHAFFDLA SAAPSPLVAY RRAGPRGEIA VDPAAARAAL VTCGGLCPGL NTVLRELVVG LHELYGVRHV FGVAAGYRGF YGTDEDHVRL DPAAVDDWHK KGGTVLKTTR GGFDLGKIVD GIVARGYTQI YAIGGDGTMR GAVAIFQEFK RRGLNISITG IPKTVDNDIG IIDRSFGFQT AVEIAQQAID AAHVEAVSAV NGVGLVKLMG RSTGHIALHA TLSSRDVDCC LIPEVDFHLE GKGGLFEFLY ERIKKKGHAV IVVAEGAGQE LIPRTDDQKR EQDESGNIVF LDVGPWLKSE LGRWWKREHP DELFTVKYID PTYMIRAVPA NATDNLYCTL LAHSAIHGVM AGFTGFVPGP VNGTYSYIPL EDVAVAKNPV DVNDHKWAWV RSVTNQPDFL KSQA //