GATY_ECOLI
ID GATY_ECOLI Reviewed; 284 AA.
AC P0C8J6; P37192; P76415;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit GatY {ECO:0000303|PubMed:8955298};
DE Short=TBPA;
DE Short=TagBP aldolase;
DE EC=4.1.2.40 {ECO:0000269|PubMed:11976750, ECO:0000305|PubMed:8955298};
DE AltName: Full=D-tagatose-bisphosphate aldolase class II;
DE AltName: Full=Tagatose-bisphosphate aldolase;
GN Name=gatY; Synonyms=yegF; OrderedLocusNames=b2096, JW5343;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 1-12, AND INDUCTION AT LOW PH.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10094700; DOI=10.1128/jb.181.7.2209-2216.1999;
RA Blankenhorn D., Phillips J., Slonczewski J.L.;
RT "Acid- and base-induced proteins during aerobic and anaerobic growth of
RT Escherichia coli revealed by two-dimensional gel electrophoresis.";
RL J. Bacteriol. 181:2209-2216(1999).
RN [5]
RP PROTEIN SEQUENCE OF 1-8.
RC STRAIN=K12;
RX PubMed=17895580; DOI=10.1266/ggs.82.291;
RA Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
RT "A role of RnlA in the RNase LS activity from Escherichia coli.";
RL Genes Genet. Syst. 82:291-299(2007).
RN [6]
RP FUNCTION, ROLE IN GALACTITOL CATABOLISM, INDUCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
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).
RN [7]
RP FUNCTION, COMPLEX WITH GATZ, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=11976750; DOI=10.1007/s00203-002-0406-6;
RA Brinkkoetter A., Shakeri-Garakani A., Lengeler J.W.;
RT "Two class II D-tagatose-bisphosphate aldolases from enteric bacteria.";
RL Arch. Microbiol. 177:410-419(2002).
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) (PubMed:8955298, PubMed:11976750). Requires GatZ subunit for full
CC activity and stability (PubMed:11976750). Is involved in the catabolism
CC of galactitol (PubMed:8955298, PubMed:11976750). Has a high aldolase
CC activity for TBP and a very low one for fructose 1,6-bisphosphate (FBP)
CC (PubMed:11976750). {ECO:0000269|PubMed:11976750,
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 Evidence={ECO:0000269|PubMed:11976750, ECO:0000305|PubMed:8955298};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22949;
CC Evidence={ECO:0000269|PubMed:11976750};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22950;
CC Evidence={ECO:0000269|PubMed:11976750};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for tagatose-1,6-bisphosphate (when expressed alone)
CC {ECO:0000269|PubMed:11976750};
CC KM=0.3 mM for tagatose-1,6-bisphosphate (when expressed with GatZ)
CC {ECO:0000269|PubMed:11976750};
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:0000305|PubMed:11976750}.
CC -!- INDUCTION: Constitutively expressed. Up-regulated under low pH
CC conditions. {ECO:0000269|PubMed:10094700, ECO:0000269|PubMed:8955298}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. TagBP aldolase GatY subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC75157.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15966.2; -; Genomic_DNA.
DR PIR; S55901; S55901.
DR RefSeq; NP_416599.2; NC_000913.3.
DR RefSeq; WP_001307281.1; NZ_SSZK01000011.1.
DR AlphaFoldDB; P0C8J6; -.
DR SMR; P0C8J6; -.
DR BioGRID; 4260432; 19.
DR ComplexPortal; CPX-6023; GatYZ tagatose-1,6-bisphosphate aldolase complex.
DR DIP; DIP-48239N; -.
DR IntAct; P0C8J6; 14.
DR STRING; 511145.b2096; -.
DR jPOST; P0C8J6; -.
DR PaxDb; P0C8J6; -.
DR PRIDE; P0C8J6; -.
DR EnsemblBacteria; AAC75157; AAC75157; b2096.
DR EnsemblBacteria; BAA15966; BAA15966; BAA15966.
DR GeneID; 946636; -.
DR KEGG; ecj:JW5343; -.
DR KEGG; eco:b2096; -.
DR PATRIC; fig|1411691.4.peg.151; -.
DR EchoBASE; EB2318; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_6; -.
DR InParanoid; P0C8J6; -.
DR OMA; NNMEIVQ; -.
DR PhylomeDB; P0C8J6; -.
DR BioCyc; EcoCyc:TAGAALDOL2-MON; -.
DR BioCyc; MetaCyc:TAGAALDOL2-MON; -.
DR SABIO-RK; P0C8J6; -.
DR UniPathway; UPA00704; UER00716.
DR PRO; PR:P0C8J6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902494; C:catalytic complex; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IC:ComplexPortal.
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 Direct protein sequencing; Galactitol metabolism; Lyase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..284
FT /note="D-tagatose-1,6-bisphosphate aldolase subunit GatY"
FT /id="PRO_0000178766"
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; 30812 MW; D414AA3921BBFE2B CRC64;
MYVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT PGTFTHAGTE
NLLALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV
VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DALYTNPAQA REFAEATGID SLAVAIGTAH
GMYASAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS
QALKNYLTEH PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA
