ID GATY_SHIDS Reviewed; 284 AA.
AC Q32EA9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit GatY;
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=Tagatose-bisphosphate aldolase;
GN Name=gatY; OrderedLocusNames=SDY_2269;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
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 -!- SEQUENCE CAUTION:
CC Sequence=ABB62346.1; Type=Erroneous initiation;
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DR EMBL; CP000034; ABB62346.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_403837.2; NC_007606.1.
DR ProteinModelPortal; Q32EA9; -.
DR STRING; 300267.SDY_2269; -.
DR EnsemblBacteria; ABB62346; ABB62346; SDY_2269.
DR GeneID; 3797037; -.
DR KEGG; sdy:SDY_2269; -.
DR PATRIC; 18694630; VBIShiDys99784_2742.
DR eggNOG; COG0191; -.
DR HOGENOM; HOG000227793; -.
DR KO; K08302; -.
DR ProtClustDB; PRK09195; -.
DR BioCyc; SDYS300267:GJEW-2265-MONOMER; -.
DR UniPathway; UPA00704; UER00716.
DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019404; P:galactitol catabolic process; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01294; TagBP_aldolase_GatY; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; Ketose_bisP_aldolase_II.
DR InterPro; IPR011288; TagBP_ald_KbaY/GatY.
DR InterPro; IPR023955; TagBP_aldolase_GatY.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01858; tag_bisphos_ald; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; FALSE_NEG.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Galactitol metabolism; Lyase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1 284 D-tagatose-1,6-bisphosphate aldolase
FT subunit GatY.
FT /FTId=PRO_0000355354.
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; 30884 MW; 101B82DE52F469A8 CRC64;
MYVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT PGTFTHAGIE
NLLALVSAMA KQYHHLLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV
VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DALYTNPVQA REFAEATGID SLAVAIGTAH
GMYASAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNSFS
QALKNYLTEH PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA
//
