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GATY_SALEP
ID   GATY_SALEP              Reviewed;         284 AA.
AC   B5QZS8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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}; OrderedLocusNames=SEN3091;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933172; CAR34667.1; -; Genomic_DNA.
DR   RefSeq; WP_000469979.1; NC_011294.1.
DR   AlphaFoldDB; B5QZS8; -.
DR   SMR; B5QZS8; -.
DR   KEGG; set:SEN3091; -.
DR   HOGENOM; CLU_040088_0_1_6; -.
DR   OMA; NNMEIVQ; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000000613; 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; 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_1000140440"
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;  30817 MW;  0C075FBC813144C6 CRC64;
     MFIISGRTML KKAQQEGYAV PAFNIHNLET LQVVVETAAE LRSPLIVAGT PGTFSYAGVG
     NIVAIAAELA KSWNHPLAVH LDHHEKLADI KMKVAAGVRS VMIDGSHFPF ADNIALVKSV
     VDYCHRYDVS VEAELGRLGG QEDDLIVDGK DALYTHPEQA REFVEKTGID SLAIAIGTAH
     GLYTAEPKLD FERLTEIRQR VDVPLVLHGA SGLPTRDITR AISLGICKVN VATELKIAFS
     GALKNYLTQH AEASDPRHYM IPAKAAMKEV VRKVIADCGC EGKL
 
 
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