ID   GATY_KLEOX              Reviewed;         284 AA.
AC   Q8VS16;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 67.
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;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN GALACTITOL AND D-TAGATOSE
RP   CATABOLISM, AND INDUCTION.
RC   STRAIN=M5a1;
RX   PubMed=15257457; DOI=10.1007/s00438-004-1022-8;
RA   Shakeri-Garakani A., Brinkkoetter A., Schmid K., Turgut S., Lengeler J.W.;
RT   "The genes and enzymes for the catabolism of galactitol, D-tagatose, and
RT   related carbohydrates in Klebsiella oxytoca M5a1 and other enteric bacteria
RT   display convergent evolution.";
RL   Mol. Genet. Genomics 271:717-728(2004).
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 and D-tagatose.
CC       {ECO:0000269|PubMed:15257457}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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.
CC   -!- SUBUNIT: Forms a complex with GatZ. {ECO:0000305}.
CC   -!- INDUCTION: By galactitol. {ECO:0000269|PubMed:15257457}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. TagBP aldolase GatY subfamily. {ECO:0000305}.
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DR   EMBL; AF416702; AAL60165.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VS16; -.
DR   SMR; Q8VS16; -.
DR   STRING; 571.MC52_04965; -.
DR   eggNOG; COG0191; Bacteria.
DR   BRENDA; 4.1.2.40; 2811.
DR   UniPathway; UPA00704; UER00716.
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   1: Evidence at protein level;
KW   Galactitol metabolism; Lyase; Metal-binding; Zinc.
FT   CHAIN           1..284
FT                   /note="D-tagatose-1,6-bisphosphate aldolase subunit GatY"
FT                   /id="PRO_0000355331"
FT   ACT_SITE        82
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..211
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..233
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  30735 MW;  07AD249C9EFC07C7 CRC64;
     MFIISSKNML LKAQRLGYAV PAFNIHNLET MQVVVETAAE LRSPLILAGT PGTYSYAGTG
     NVVAIARDLA KIWDLPLAVH LDHHEDLADI TRKVQAGIRS VMIDGSHSPF EENVALVKSV
     VELSHRYDAS VEAELGRLGG VEDDLGVDAK DALYTNPEQG REFVARTGID SLAVVIGTAH
     GLYAAEPKLG FAALPPISER VDVPLVLHGA SKLPDSDIRR AISLGVCKVN VATELKIAFS
     DALKHYFEEN PDANEPRHYM KPAKAAMKDV VRKVIHVCGC EGQL