AC MF_00339; DC Protein; auto TR HAMAP; MF_00339; -; 1; level=0 XX Names: Phosphofructokinase_I_B1 XX 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; XX 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub- CC 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; TIGR02482; PFKA_ATP; 1; trigger=no DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1; trigger=no XX KW Allosteric enzyme KW Cytoplasm KW Kinase KW Transferase KW Glycolysis KW ATP-binding KW Nucleotide-binding 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: PFKA_ECOLI (P0A796) FT BINDING 73..74 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R-x FT BINDING 103..106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-[DEN]-G-[ST] FT BINDING 22..26 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT Condition: R-x(3)-[RK] FT BINDING 55..60 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT Optional; Condition: R-Y-x(2)-S-[DE] FT BINDING 126..128 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: [TS]-x-D FT BINDING 170..172 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: M-G-[RHN] FT BINDING 186..188 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: G-x-[ED] FT BINDING 214..216 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: K-x(2) FT BINDING 250..253 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 128 FT /note="Proton acceptor" FT Condition: D FT BINDING 104 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Condition: [DEN] FT BINDING 12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G FT BINDING 155 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: [RK] FT BINDING 163 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT Condition: R FT BINDING 212 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Optional; Condition: [RK] FT BINDING 223 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: E FT BINDING 244 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT Condition: [RK] XX Size: 319-361; Related: None; Template: P0A796; P00512; P0DOB6; Q9WY52; P21777; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in BACTN 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 1.45 2023/06/01 //