AC MF_02067; DC Protein; auto TR HAMAP; MF_02067; -; 1; level=0 XX Names: FBP_aldolase_phosphatase XX ID FBPAP DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase; DE Short=FBP A/P; DE Short=FBP aldolase/phosphatase; DE EC=3.1.3.11; DE EC=4.1.2.13; GN Name=fbp; XX CC -!- FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol CC condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3- CC phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the CC dephosphorylation of FBP to fructose-6-phosphate (F6P). CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6- CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Homooctamer; dimer of tetramers. CC -!- DOMAIN: Consists of a single catalytic domain, but remodels its active- CC site architecture via a large structural change to exhibit dual CC activities. CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family. XX DR Pfam; PF01950; FBPase_3; 1; trigger=no DR PIRSF; PIRSF015647; FBPtase_archl; 1; trigger=no XX KW Carbohydrate metabolism KW Gluconeogenesis KW Hydrolase KW Lyase KW Magnesium KW Metal-binding KW Schiff base XX GO GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity GO GO:0004332; F:fructose-bisphosphate aldolase activity GO GO:0000287; F:magnesium ion binding GO GO:0006094; P:gluconeogenesis XX FT From: FBPAP_SULTO (F9VMT6) FT BINDING 103..104 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Optional; Condition: G-N FT BINDING 241..242 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT Optional; Condition: Q-[HSK] FT ACT_SITE 11 FT /note="Proton acceptor; for FBP phosphatase activity" FT Condition: D FT ACT_SITE 228 FT /note="Proton donor/acceptor; for FBP aldolase activity" FT Condition: Y FT ACT_SITE 231 FT /note="Schiff-base intermediate with DHAP; for FBP aldolase FT activity" FT Condition: K FT BINDING 11 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 18 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: H FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 53 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 94 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: Q FT BINDING 131 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT Condition: K FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT Condition: D FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT Condition: D FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT Condition: D FT BINDING 18 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Optional; Condition: H FT BINDING 18 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT Optional; Condition: H FT BINDING 90 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Optional; Condition: Y FT BINDING 132 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Optional; Condition: K FT BINDING 132 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT Optional; Condition: K FT BINDING 265 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Optional; Condition: R FT BINDING 265 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT Optional; Condition: R FT BINDING 286 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Optional; Condition: D FT BINDING 286 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT Optional; Condition: D FT BINDING 347 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Optional; Condition: Y XX Size: 360-410; Related: None; Template: F9VMT6; B1YAL1; Q2RG86; Q72K02; A0RV30; A8A9E4; A4YIZ5; D9PUH5; Q8NKR9; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.9 2022/11/19 //