AC MF_01293; DC Protein; auto TR HAMAP; MF_01293; -; 1; level=0 XX Names: TagBP_aldolase_KbaY XX ID KBAY DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit KbaY; DE Short=TBPA; DE Short=TagBP aldolase; DE EC=4.1.2.40; DE AltName: Full=D-tagatose-bisphosphate aldolase class II; DE AltName: Full=Ketose 1,6-bisphosphate aldolase class II; DE AltName: Full=Tagatose-bisphosphate aldolase; GN Name=kbaY; XX CC -!- FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase CC KbaYZ, which catalyzes the reversible aldol condensation of CC dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with CC glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate CC (TBP). Requires KbaZ subunit for full activity and stability. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:22948, CC ChEBI:CHEBI:57642, ChEBI:CHEBI:58694, ChEBI:CHEBI:59776; EC=4.1.2.40; case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case CC -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; CC D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6- CC phosphate: step 2/2. CC -!- SUBUNIT: Homotetramer. Forms a complex with KbaZ. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. TagBP aldolase KbaY subfamily. XX DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1; trigger=no DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1; trigger=no DR Pfam; PF01116; F_bP_aldolase; 1; trigger=no DR NCBIfam; TIGR00167; CbbA; 1; trigger=no DR NCBIfam; TIGR01858; Tag_bisphos_ald; 1; trigger=no XX KW Lyase case KW Metal-binding KW Zinc end case XX case GO GO:0008270; F:zinc ion binding end case GO GO:0009025; F:tagatose-bisphosphate aldolase activity GO GO:0005975; P:carbohydrate metabolic process XX FT From: KBAY_ECOLI (P0AB74) FT BINDING 230..233 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT Condition: N-x-A-T FT BINDING 209..211 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT Condition: G-x-S FT ACT_SITE 82 FT /note="Proton donor" FT Condition: D FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 208 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 181 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT Condition: G XX Size: 286-292; Related: MF_01294; Template: P0AB74; Q9KIP8; Scope: Bacteria; Enterobacterales Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Subunit kbaZ is described in MF_01295. In some enterobacteria, a second D-tagatose-1,6-bisphosphate aldolase is present: gatYZ (MF_01294 and MF_01296). XX # Revision 1.14 2023/06/01 //