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GATY_ECO55
ID   GATY_ECO55              Reviewed;         284 AA.
AC   B7L9W7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=EC55989_2351;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAU98222.1; -; Genomic_DNA.
DR   RefSeq; WP_000338050.1; NC_011748.1.
DR   AlphaFoldDB; B7L9W7; -.
DR   SMR; B7L9W7; -.
DR   EnsemblBacteria; CAU98222; CAU98222; EC55989_2351.
DR   KEGG; eck:EC55989_2351; -.
DR   HOGENOM; CLU_040088_0_1_6; -.
DR   OMA; NNMEIVQ; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000000746; 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_1000165279"
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;  30786 MW;  4C2E0EA22A671135 CRC64;
     MCVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT PGTFTHAGTE
     NLLALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV
     VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DAFYTNPAQA REFAEATGID SLAVAIGTAH
     GMYASAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS
     QALKNYLTEH PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA
 
 
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