ID KBAY_ECOL5 Reviewed; 286 AA. AC Q0TCW8; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 02-SEP-2026, entry version 108. DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit KbaY {ECO:0000255|HAMAP-Rule:MF_01293}; DE Short=TBPA {ECO:0000255|HAMAP-Rule:MF_01293}; DE Short=TagBP aldolase {ECO:0000255|HAMAP-Rule:MF_01293}; DE EC=4.1.2.40 {ECO:0000255|HAMAP-Rule:MF_01293}; DE AltName: Full=D-tagatose-bisphosphate aldolase class II {ECO:0000255|HAMAP-Rule:MF_01293}; DE AltName: Full=Ketose 1,6-bisphosphate aldolase class II {ECO:0000255|HAMAP-Rule:MF_01293}; DE AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000255|HAMAP-Rule:MF_01293}; GN Name=kbaY {ECO:0000255|HAMAP-Rule:MF_01293}; GN OrderedLocusNames=ECP_3229; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=536 / UPEC; RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). 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 {ECO:0000255|HAMAP-Rule:MF_01293}. 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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01293}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01293}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01293}; 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. {ECO:0000255|HAMAP-Rule:MF_01293}. CC -!- SUBUNIT: Homotetramer. Forms a complex with KbaZ. {ECO:0000255|HAMAP- CC Rule:MF_01293}. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. TagBP aldolase KbaY subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01293}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000247; ABG71211.1; -; Genomic_DNA. DR RefSeq; WP_000022766.1; NC_008253.1. DR AlphaFoldDB; Q0TCW8; -. DR SMR; Q0TCW8; -. DR GeneID; 75173310; -. DR GeneID; 75203745; -. DR KEGG; ecp:ECP_3229; -. DR HOGENOM; CLU_040088_0_1_6; -. DR UniPathway; UPA00704; UER00716. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00453; FTBP_aldolase_II; 1. DR FunFam; 3.20.20.70:FF:000043; D-tagatose-1,6-bisphosphate aldolase subunit GatY; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01293; TagBP_aldolase_KbaY; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR023788; TagBP_ald_KbaY. DR InterPro; IPR011288; TagBP_ald_KbaY/GatY. DR NCBIfam; TIGR00167; cbbA; 1. DR NCBIfam; NF006626; PRK09195.1; 1. DR NCBIfam; NF009374; PRK12737.1; 1. DR NCBIfam; NF009375; PRK12738.1; 1. DR NCBIfam; TIGR01858; tag_bisphos_ald; 1. DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. PE 3: Inferred from homology; KW Lyase; Metal-binding; Zinc. FT CHAIN 1..286 FT /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaY" FT /id="PRO_0000355327" FT ACT_SITE 82 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293" FT BINDING 181 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293" FT BINDING 208 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293" FT BINDING 209..211 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293" FT BINDING 230..233 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293" SQ SEQUENCE 286 AA; 31294 MW; CAA42DF05C2B918B CRC64; MSIISTKYLL QDAQANGYAV PAFNIHNAET IQAILEVCSE MRSPVILAGT PGTFKHIALE EIYALCSAYS TTYNMPLALH LDHHESLDDI RRKVHAGVRS AMIDGSHFPF AENVKLVKSV VDFCHSQDCS VEAELGRLGG VEDDMSVDAE SAFLTDPQEA KRFVELTGVD SLAVAIGTAH GLYSKTPKID FQRLAEIREV VDVPLVLHGA SDVPDEFVRR TIELGVTKVN VATELKIAFA GAVKAWFAEN PQGNDPRYYM RVGMDAMKEV VRNKINVCGS ANRISA //