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GATY_SALTI
ID   GATY_SALTI              Reviewed;         284 AA.
AC   Q8XGZ9; Q7AM79;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit GatY {ECO:0000255|HAMAP-Rule:MF_01294};
DE            Short=TBPA {ECO:0000255|HAMAP-Rule:MF_01294};
DE            Short=TagBP aldolase {ECO:0000255|HAMAP-Rule:MF_01294};
DE            EC=4.1.2.40 {ECO:0000255|HAMAP-Rule:MF_01294};
DE   AltName: Full=D-tagatose-bisphosphate aldolase class II {ECO:0000255|HAMAP-Rule:MF_01294};
DE   AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000255|HAMAP-Rule:MF_01294};
GN   Name=gatY {ECO:0000255|HAMAP-Rule:MF_01294};
GN   OrderedLocusNames=STY3435, t3173;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
CC   -!- FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase
CC       GatYZ, 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 GatZ subunit for full activity and stability. Is
CC       involved in the catabolism of galactitol. {ECO:0000255|HAMAP-
CC       Rule:MF_01294}.
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_01294};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01294};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01294};
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_01294}.
CC   -!- SUBUNIT: Forms a complex with GatZ. {ECO:0000255|HAMAP-Rule:MF_01294}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. TagBP aldolase GatY subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01294}.
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DR   EMBL; AE014613; AAO70712.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD07775.1; -; Genomic_DNA.
DR   RefSeq; NP_457638.1; NC_003198.1.
DR   RefSeq; WP_000469985.1; NZ_WSUR01000003.1.
DR   AlphaFoldDB; Q8XGZ9; -.
DR   SMR; Q8XGZ9; -.
DR   STRING; 220341.16504324; -.
DR   EnsemblBacteria; AAO70712; AAO70712; t3173.
DR   KEGG; stt:t3173; -.
DR   KEGG; sty:STY3435; -.
DR   PATRIC; fig|220341.7.peg.3497; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_040088_0_1_6; -.
DR   OMA; TVGGMED; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
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:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019404; P:galactitol catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00947; TBP_aldolase_IIB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01294; TagBP_aldolase_GatY; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_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; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
KW   Galactitol metabolism; Lyase; Metal-binding; Zinc.
FT   CHAIN           1..284
FT                   /note="D-tagatose-1,6-bisphosphate aldolase subunit GatY"
FT                   /id="PRO_0000355350"
FT   ACT_SITE        82
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01294"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01294"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01294"
FT   BINDING         181
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01294"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01294"
FT   BINDING         209..211
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01294"
FT   BINDING         230..233
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01294"
SQ   SEQUENCE   284 AA;  30922 MW;  0AAAD91D4CBD80FF CRC64;
     MFIISSKNML QKAQHAGYAV PAFNIHNLET LQVVVETAAE MRSPLIVAGT PGTFSYAGMG
     NIVAIAGDLA REYNLPLAIH LDHHESLADI ESKVMAGIRS VMIDGSHFPF EENVALVKSV
     VDFCHRYDTS VEAELGRLGG IEDDLVVDSK DALYTNPQQA REFVARTGID SLAVAIGTAH
     GMYAAEPKLD FERLAEIRAL VDIPLVLHGA SGLPESDIRQ AISLGVCKVN VATELKIAFS
     DALKEYFLQN PKANDPRHYM QPAKQAMKEV VRKVIHVCGC EGQL
 
 
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