GATY_ECOLX
ID GATY_ECOLX Reviewed; 284 AA.
AC P0C8J7; P37192; P76415;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
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 Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EC3132;
RX PubMed=7772602; DOI=10.1016/0167-4781(95)00053-j;
RA Nobelmann B., Lengeler J.W.;
RT "Sequence of the gat operon for galactitol utilization from a wild-type
RT strain EC3132 of Escherichia coli.";
RL Biochim. Biophys. Acta 1262:69-72(1995).
RN [2]
RP FUNCTION AS A TAGBP ALDOLASE, ROLE IN GALACTITOL CATABOLISM, AND INDUCTION.
RC STRAIN=EC3132;
RX PubMed=8955298; DOI=10.1128/jb.178.23.6790-6795.1996;
RA Nobelmann B., Lengeler J.W.;
RT "Molecular analysis of the gat genes from Escherichia coli and of their
RT roles in galactitol transport and metabolism.";
RL J. Bacteriol. 178:6790-6795(1996).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:8955298}.
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:0000250}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:8955298}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. TagBP aldolase GatY subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56226.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X79837; CAA56226.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P0C8J7; -.
DR SMR; P0C8J7; -.
DR IntAct; P0C8J7; 1.
DR MINT; P0C8J7; -.
DR STRING; 585034.ECIAI1_2170; -.
DR eggNOG; COG0191; Bacteria.
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; PS00602; ALDOLASE_CLASS_II_1; 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_0000355330"
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; 30816 MW; 859FD88CE7B4C8B3 CRC64;
MYVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT PGTFTHAGTE
NLLALVSAMA KQYHHPLAIH LDHHTKFDDI AQNLRSGVRS VMIDASHLPF AQNISRVKEV
VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DAFYTNPAQA REFAEATGID SLAVAIGTAH
GMYASAPVLD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS
QALKNYLTAH PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA
