ID GATY_SHISS Reviewed; 284 AA. AC Q3Z0B4; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 16-JUN-2009, entry version 24. DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit gatY; 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; GN Name=gatY; OrderedLocusNames=SSON_2144; OS Shigella sonnei (strain Ss046). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). CC -!- FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate CC aldolase gatYZ, 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 gatZ subunit for full activity and CC stability. Is involved in the catabolism of galactitol (By CC 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: Forms a complex with gatZ (By similarity). CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. TagBP aldolase gatY 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; CP000038; AAZ88798.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_311033.2; -. DR GeneID; 3666959; -. DR GenomeReviews; CP000038_GR; SSON_2144. DR KEGG; ssn:SSON_2144; -. DR HOGENOM; Q3Z0B4; -. DR BioCyc; SSON300269:SSO_2144-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:0019404; P:galactitol catabolic process; IEA:HAMAP. 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_01294; -; 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; Galactitol metabolism; Lyase; Metal-binding; Zinc. FT CHAIN 1 284 D-tagatose-1,6-bisphosphate aldolase FT subunit gatY. FT /FTId=PRO_0000355357. 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 284 AA; 30900 MW; AA65FD2A117EF434 CRC64; MYVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT PGTFTYAGTE NLLALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DVFYTNPAQA REFAEATGID SLAVAIGTAH GMYASAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS QALKNYLTEH PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA //