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GATY_ECOL5
ID   GATY_ECOL5              Reviewed;         284 AA.
AC   Q0TFZ6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=ECP_2134;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG70133.1; -; Genomic_DNA.
DR   RefSeq; WP_000289808.1; NC_008253.1.
DR   AlphaFoldDB; Q0TFZ6; -.
DR   SMR; Q0TFZ6; -.
DR   STRING; 362663.ECP_2134; -.
DR   EnsemblBacteria; ABG70133; ABG70133; ECP_2134.
DR   KEGG; ecp:ECP_2134; -.
DR   HOGENOM; CLU_040088_0_1_6; -.
DR   OMA; NNMEIVQ; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000009182; 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_0000355337"
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;  30980 MW;  D41E361BCCC3B1B2 CRC64;
     MYVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAS MHAPVIIAGT PGTFTHVGTE
     NLMALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV
     VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DAFYTNPVQA REFAEATGID SLAVAIGTAH
     GMYARAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS
     QALKNYLTEH PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA
 
 
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