AC MF_01979; DC Protein; auto TR HAMAP; MF_01979; -; 1; level=0 XX Names: Phosphofructokinase_II_Short XX ID PFP DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase; DE EC=2.7.1.90; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent; DE AltName: Full=PPi-dependent phosphofructokinase; DE Short=PPi-PFK; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase; case GN Name=pfp; end case XX 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 -!- 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 -!- ACTIVITY REGULATION: Non-allosteric. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. case CC -!- SUBUNIT: Homodimer. else case CC -!- SUBUNIT: Homotetramer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily. XX DR Pfam; PF00365; PFK; 1; trigger=no DR PIRSF; PIRSF036482; PPi_PFK_TM0289; 1; trigger=no DR PRINTS; PR00476; PHFRCTKINASE; 1; trigger=no XX KW Cytoplasm KW Kinase KW Transferase KW Glycolysis KW Magnesium KW Metal-binding XX GO GO:0003872; F:6-phosphofructokinase activity GO GO:0006096; P:glycolytic process GO GO:0005737; C:cytoplasm XX FT From: PFP_THEMA (Q9WYC5) FT SITE 108 FT /note="Important for catalytic activity and substrate FT specificity; stabilizes the transition state when the FT phosphoryl donor is PPi; prevents ATP from binding by FT mimicking the alpha-phosphate group of ATP" FT Condition: D FT BINDING 132..134 FT /ligand="substrate" FT Condition: T-x-D FT BINDING 178..180 FT /ligand="substrate" FT Condition: M-G-R FT BINDING 300..303 FT /ligand="substrate" FT Condition: Y-x(2)-R FT ACT_SITE 134 FT /note="Proton acceptor" FT Condition: D FT BINDING 107 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Condition: D FT BINDING 238 FT /ligand="substrate" FT Condition: E FT BINDING 12 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT Condition: G FT SITE 131 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT Condition: K XX Size: 411-476; Related: None; Template: Q9WYC5; Q27705; A2E9H3; Scope: Bacteria Eukaryota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Classification of type A phosphofructokinases into subfamilies was done according to Mueller at al.(2001) (PubMed:11673446) and Bapteste et al.(2003) (PubMed:14585511). XX # Revision 1.11 2022/11/19 //