ID B5YIA7_THEYD Unreviewed; 411 AA. AC B5YIA7; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01979}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01979}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01979}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01979}; DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01979}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01979}; GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01979}; GN OrderedLocusNames=THEYE_A1948 {ECO:0000313|EMBL:ACI21803.1}; OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87). OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales; OC Thermodesulfovibrionaceae; Thermodesulfovibrio. OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI21803.1, ECO:0000313|Proteomes:UP000000718}; RN [1] {ECO:0000313|Proteomes:UP000000718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51303 / DSM 11347 / YP87 RC {ECO:0000313|Proteomes:UP000000718}; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain RT ATCC 51303 / DSM 11347 / YP87."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACI21803.1, ECO:0000313|Proteomes:UP000000718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51303 / DSM 11347 / YP87 RC {ECO:0000313|Proteomes:UP000000718}; RX PubMed=25635016; RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M., RA Robb F.T., Ward N.L., Eisen J.A.; RT "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium RT Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae)."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as CC phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible, CC and can thus function both in glycolysis and gluconeogenesis. CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. CC {ECO:0000256|ARBA:ARBA00003138, ECO:0000256|HAMAP-Rule:MF_01979}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; CC Evidence={ECO:0000256|ARBA:ARBA00000628, ECO:0000256|HAMAP- CC Rule:MF_01979}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_01979}; CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01979}. 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_01979}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01979}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01979}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01979}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01979}. 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; CP001147; ACI21803.1; -; Genomic_DNA. DR RefSeq; WP_012546508.1; NC_011296.1. DR RefSeq; YP_002249738.1; NC_011296.1. DR AlphaFoldDB; B5YIA7; -. DR STRING; 289376.THEYE_A1948; -. DR EnsemblBacteria; ACI21803; ACI21803; THEYE_A1948. DR KEGG; tye:THEYE_A1948; -. DR PATRIC; fig|289376.4.peg.1903; -. DR eggNOG; COG0205; Bacteria. DR HOGENOM; CLU_020655_0_0_0; -. DR InParanoid; B5YIA7; -. DR OrthoDB; 9802503at2; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000718; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR GO; GO:0009749; P:response to glucose; IBA:GO_Central. DR Gene3D; 3.40.50.450; -; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 1. DR HAMAP; MF_01979; Phosphofructokinase_II_Short; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR InterPro; IPR011403; PPi-PFK_TM0289. DR NCBIfam; NF041103; PFKA_PPi_Ttgales; 1. DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1. DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF036482; PPi_PFK_TM0289; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01979}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01979}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01979}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01979}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01979}; Reference proteome {ECO:0000313|Proteomes:UP000000718}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01979}. FT DOMAIN 4..323 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 133 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" FT BINDING 11 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" FT BINDING 106 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" FT BINDING 131..133 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" FT BINDING 177..179 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" FT BINDING 238 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" FT BINDING 298..301 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" FT SITE 130 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979" SQ SEQUENCE 411 AA; 45779 MW; 163B1B13E752A258 CRC64; METVGIIVGG GPAPGINGTI SAATIEAINQ GKKVIGIKGG FKPLFDGNLS CAMPLSVDDV SRIHTKGGSI LRTSREHAER VKEKFPVLME TLKKLGIKYL ITIGGDGTLF MANWIEREAR GEINVVHVPK TIDNDLPLPG GASTFGYETA RHWGVEIVKN IMEDARVSAR WYFLTIMGRY TGHLALGVGK AAGATLTIIP EEFPEEKISF KKVADILTGA IIKRLSMGRD HGVVIMAEGL SEKFDPEELS HYEQLEKDET GRVRLSEIQL GRIMKNFVKK SLEDMGIKLT IVDKNIGYEL RSADPIPYDI EYTRNLGYGA VRYLLRGGTG AMITFEEGHL RPIPFVELID YRTGKVKIRK VDITSENYEV GRKYMIRLEA EDFEGERLKG LASVVKMSEK EFREKFFYVT T //