ID C5XJ72_SORBI Unreviewed; 561 AA. AC C5XJ72; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 79. 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_3003G290000 {ECO:0000313|EMBL:EES03580.1}; 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:EES03580.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EES03580.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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|EMBL:EES03580.1} RP NUCLEOTIDE SEQUENCE. RA Paterson A., Mullet J., Bowers J., 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., Chapman J., Feltus F., RA Gowik U., Grigoriev I., Lyons E., Maher C., Martis M., Narechania A., RA Otillar R., Penning B., Salamov A., Wang Y., Zhang L., Carpita N., RA Freeling M., Gingle A., Hash C., Keller B., Klein P., Kresovich S., RA Mccann M., Ming R., Peterson D., Rahman M., Ware D., Westhoff P., Mayer K., RA Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.; RT "WGS assembly of Sorghum bicolor."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. 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; CM000762; EES03580.1; -; Genomic_DNA. DR RefSeq; XP_002458460.1; XM_002458415.1. DR AlphaFoldDB; C5XJ72; -. DR EnsemblPlants; EES03580; EES03580; SORBI_3003G290000. DR GeneID; 8062161; -. DR Gramene; EES03580; EES03580; SORBI_3003G290000. DR KEGG; sbi:8062161; -. DR HOGENOM; CLU_020655_7_2_1; -. DR OMA; TRDERPM; -. DR OrthoDB; 350658at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000768; Chromosome 3. DR ExpressionAtlas; C5XJ72; baseline and differential. 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: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:SF15; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1. DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 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 174..479 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 541..561 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 300 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 244..245 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 269..272 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 298..300 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 343..345 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 399 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT BINDING 455..458 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" FT SITE 271 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186" SQ SEQUENCE 561 AA; 61494 MW; 67CCBEA64492641A CRC64; MASSHIILPK EEEEEEKEAA AVAEAGLGVG VEADHDSPAQ RPYQEQAPGK AALPFSATCV RISRDSYPNL RALRNASTMA LHDDDAAFVK IEEGDFGYVL DDVPHLTDYL PDLPTFPNPL QDHPAYSTVK QYFVNADDTV PEKVVVQKNS PRGVHFRRAG PRQRVYFESE EVKACIVTCG GLCPGLNTVI RELVCGLSHM YNVSNVFGIQ NGYKGFYSSN YLPMTPKSVN DIHKRGGTVL GTSRGGHDTK KIVDNIQDRG INQVYIIGGD GTQKGAYEIY KEIRRRGLHV AVAGIPKTID NDIAVIDKSF GFDTAVEEAQ RAINAAHVEA SSAENGIGLV KLMGRYSGFI AMYATLASRD VDCCLIPESP FYLEGEGGLF EYIDRRLKEN NHMVIVVAEG AGQDLIAQSI PAADQQDASG NKLLLDVGLW LTHKIKDYCK SKKMEMTIKY IDPTYMIRAI PSNASDNVYC TLLAHSAIHG AMAGYSFTVG MVNGRHAYIP FHRVTSTRNK VRITDRMWAR LLSSTNQPSF LSQKDIDAAR EADKAANAKN QSAPALANGE K //