AC MF_01980; DC Protein; auto c? TR HAMAP; MF_01980; -; 1; level=0 XX Names: Phosphofructokinase_II_Long 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=Probable 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 PFKA DE RecName: Full=6-phosphofructokinase; DE EC=2.7.1.-; GN Name=pfk; 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily. XX DR Pfam; PF00365; PFK; 1; trigger=no DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1; trigger=no DR PRINTS; PR00476; PHFRCTKINASE; 1; trigger=no DR NCBIfam; TIGR02477; PFKA_PPi; 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_BORBU (P70826) FT SITE 177 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 Optional; Condition: D FT SITE 177 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT Optional; Condition: G case FT BINDING 82 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT Condition: G FT SITE 203 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT Condition: K else case FT BINDING 146..147 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [RK]-x FT BINDING 175..178 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-[DE]-G-[ST] FT BINDING 82 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G end case case or FT BINDING 204..206 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: T-x-D FT BINDING 243..244 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT Optional; Condition: K-Y FT BINDING 251..253 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: M-G-[RH] FT BINDING 428..431 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 206 FT /note="Proton acceptor" FT Condition: D FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Condition: [DE] FT BINDING 312 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: E end case XX Size: 548-573; Related: MF_03185; Template: P70826; C4LZC2; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in CHLTR 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-177 (PFP_BORBU 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 //