GATY_SALPC
ID GATY_SALPC Reviewed; 284 AA.
AC C0PZ24;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=SPC_3327;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(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; CP000857; ACN47412.1; -; Genomic_DNA.
DR RefSeq; WP_000469979.1; NC_012125.1.
DR AlphaFoldDB; C0PZ24; -.
DR SMR; C0PZ24; -.
DR EnsemblBacteria; ACN47412; ACN47412; SPC_3327.
DR KEGG; sei:SPC_3327; -.
DR HOGENOM; CLU_040088_0_1_6; -.
DR OMA; NNMEIVQ; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000001599; 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_1000165280"
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
