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 16-JUN-2009, entry version 20. DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit kbaY; DE Short=TagBP aldolase; DE Short=TBPA; DE EC=4.1.2.40; DE AltName: Full=Tagatose-bisphosphate aldolase; DE AltName: Full=D-tagatose-bisphosphate aldolase class II; DE AltName: Full=Ketose 1,6-bisphosphate aldolase class II; GN Name=kbaY; OrderedLocusNames=ECP_3229; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 CC aldolase kbaYZ, which catalyzes the reversible aldol condensation CC of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with CC glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6- CC bisphosphate (TBP). Requires kbaZ subunit for full activity and CC stability (By similarity). CC -!- CATALYTIC ACTIVITY: D-tagatose 1,6-bisphosphate = glycerone CC phosphate + D-glyceraldehyde 3-phosphate. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate CC degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate CC from D-tagatose 6-phosphate: step 2/2. CC -!- SUBUNIT: Homotetramer. Forms a complex with kbaZ (By similarity). CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. TagBP aldolase kbaY subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000247; ABG71211.1; -; Genomic_DNA. DR RefSeq; YP_671112.1; -. DR SMR; Q0TCW8; 2-284. DR GeneID; 4188585; -. DR GenomeReviews; CP000247_GR; ECP_3229. DR KEGG; ecp:ECP_3229; -. DR HOGENOM; Q0TCW8; -. DR OMA; Q0TCW8; TIELGVC. DR BioCyc; ECOL362663:ECP_3229-MON; -. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro. DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolysis; IEA:InterPro. DR GO; GO:0019512; P:lactose catabolic process via tagatose-6-ph...; IEA:InterPro. DR HAMAP; MF_01293; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; Ketose_bisP_aldolase_II. DR InterPro; IPR011288; Tag_bisphos_ald. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR ProDom; PD002376; K_bP_aldolase; 1. DR TIGRFAMs; TIGR00167; cbbA; 1. DR TIGRFAMs; TIGR01858; tag_bisphos_ald; 1. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Metal-binding; Zinc. FT CHAIN 1 286 D-tagatose-1,6-bisphosphate aldolase FT subunit kbaY. FT /FTId=PRO_0000355327. FT REGION 209 211 Dihydroxyacetone phosphate binding (By FT similarity). FT REGION 230 233 Dihydroxyacetone phosphate binding (By FT similarity). FT ACT_SITE 82 82 Proton donor (By similarity). FT METAL 83 83 Zinc; catalytic (By similarity). FT METAL 180 180 Zinc; catalytic (By similarity). FT METAL 208 208 Zinc; catalytic (By similarity). FT BINDING 181 181 Dihydroxyacetone phosphate; via amide FT nitrogen (By similarity). 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 //