GATY_SHIBS
ID GATY_SHIBS Reviewed; 284 AA.
AC Q323C6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
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=SBO_0917;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB65582.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000036; ABB65582.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000558570.1; NC_007613.1.
DR AlphaFoldDB; Q323C6; -.
DR SMR; Q323C6; -.
DR EnsemblBacteria; ABB65582; ABB65582; SBO_0917.
DR KEGG; sbo:SBO_0917; -.
DR HOGENOM; CLU_040088_0_1_6; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000007067; 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_0000355353"
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; 30834 MW; 21E90C6B76F10531 CRC64;
MHVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT PGTFTHAGTE
NLLALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV
VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DAFYTNPAQA REFAEATGID SLAVAIGTAH
GMYASAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS
QALKNYLTEH PEATEPRDYL QSAKSAMRDV VSKVIADCGC EGRA
