AC MF_01976; DC Protein; auto TR HAMAP; MF_01976; -; 1; level=0 XX Names: Phosphofructokinase_III XX case 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; GN Name=pfp; else case ID PFKA DE RecName: Full=ATP-dependent 6-phosphofructokinase; DE Short=ATP-PFK; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; GN Name=pfkA; else ID PFP DE RecName: Full=6-phosphofructokinase; DE EC=2.7.1.-; end case XX case 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. else case 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. 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; else CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to CC fructose 1,6-bisphosphate, the first committing step of glycolysis. end case 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. CC -!- SUBUNIT: Homodimer or homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC Mixed-substrate PFK group III subfamily. XX DR Pfam; PF00365; PFK; 1; trigger=no DR PIRSF; PIRSF000532; ATP_PFK_prok; 1; trigger=no DR PRINTS; PR00476; PHFRCTKINASE; 1; trigger=no DR NCBIfam; TIGR02483; PFK_mixed; 1; trigger=no DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1; trigger=no XX KW Cytoplasm KW Kinase KW Transferase KW Glycolysis KW Magnesium KW Metal-binding case KW ATP-binding KW Nucleotide-binding end case XX GO GO:0003872; F:6-phosphofructokinase activity GO GO:0006096; P:glycolytic process GO GO:0005737; C:cytoplasm XX FT From: PFP_AMYME (Q59126) FT SITE 104 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 Tag: PPI; Optional; Condition: D FT SITE 104 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT Tag: ATP; Optional; Condition: G FT BINDING 125..127 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: T-x-D FT BINDING 169..171 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: M-G-[RH] FT BINDING 271..274 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: [HY]-x(2)-R FT ACT_SITE 127 FT /note="Proton acceptor" FT Condition: D FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Condition: [DEN] FT BINDING 162 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT Optional; Condition: R FT BINDING 221 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: E FT BINDING 265 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT Optional; Condition: [RK] case FT BINDING 10 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT Condition: G FT SITE 124 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT Condition: K end case FT From: PFKA2_STRCO (Q9L1L8) case FT BINDING 72..73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [RK]-x FT BINDING 102..105 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-[DEN]-G-[ST] FT BINDING 10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G end case XX Size: 336-384; Related: None; Template: Q59126; Q9L1L8; Scope: Archaea Bacteria Fusion: Nter: None Cter: None Duplicate: in NOSS1, STRCO, SYNY3 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). Phosphoryl donor specificity (ATP or PPi) seems to be determined by a single residue, Asp or Gly-104 (PFP_AMYME numbering) according to Chi et al.(2000) (PubMeed:11001940), Moore et al.(2002) (PubMed:12015149), and Bapteste et al.(2003) (PubMed:14585511) and references therein. XX # Revision 1.13 2023/06/01 //