ID KBAY_ECOUT Reviewed; 286 AA. AC Q1R6K0; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-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=UTI89_C3568; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE09014.1; -; Genomic_DNA. DR RefSeq; YP_542545.1; -. DR SMR; Q1R6K0; 2-284. DR GeneID; 3992479; -. DR GenomeReviews; CP000243_GR; UTI89_C3568. DR KEGG; eci:UTI89_C3568; -. DR HOGENOM; Q1R6K0; -. DR OMA; Q1R6K0; TIELGVC. DR BioCyc; ECOL364106:UTI89_C3568-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_0000355324. 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 //