AC MF_03184; DC Protein; auto TR HAMAP; MF_03184; -; 1; level=0 XX Names: Phosphofructokinase_I_E 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; 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, AMP, or fructose CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. case CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains. else case CC -!- SUBUNIT: Homo- and heterotetramers. else CC -!- SUBUNIT: Homotetramer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' CC sub-subfamily. XX DR Pfam; PF00365; PFK; 2; trigger=no DR PIRSF; PIRSF000533; ATP_PFK_euk; 1; trigger=no DR PRINTS; PR00476; PHFRCTKINASE; 1; trigger=no DR NCBIfam; TIGR02478; 6PF1K_euk; 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: PFKA1_YEAST (P16861) FT BINDING 278..279 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R-x FT BINDING 308..311 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-[DE]-G-[ST] FT REGION Nter..580 FT /note="N-terminal catalytic PFK domain 1" FT BINDING 354..356 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: S-x-D FT BINDING 398..400 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: M-G-R FT BINDING 488..491 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: H-x(2)-R FT REGION 581..594 FT /note="Interdomain linker" FT REGION 595..Cter FT /note="C-terminal regulatory PFK domain 2" FT BINDING 722..726 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: [TS]-[ILMV]-S-N-N FT BINDING 767..769 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: [MQ]-G-[GA] FT BINDING 859..862 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: H-x-Q-Q FT ACT_SITE 356 FT /note="Proton acceptor" FT Condition: D FT BINDING 309 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Condition: [DE] FT BINDING 215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G FT BINDING 391 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT Condition: R FT BINDING 455 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: E FT BINDING 482 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT Condition: [RK] FT BINDING 665 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: [RK] FT BINDING 760 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT Condition: R FT BINDING 827 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: [ED] FT BINDING 853 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT Condition: [RK] FT BINDING 952 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_note="allosteric activator; ligand shared FT between dimeric partners" FT /note="in other chain" FT Condition: R XX Size: 756-992; Related: None; Template: P16861; P16862; P90521; P17858; P08237; P00511; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in CANAX, KLULA, PICPA, PICPG, YEAST 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 1.14 2023/06/01 //