TAGAD_SALTY
ID TAGAD_SALTY Reviewed; 398 AA.
AC Q8ZL58;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=L-talarate/galactarate dehydratase {ECO:0000303|PubMed:17649980};
DE Short=TalrD/GalrD {ECO:0000303|PubMed:17649980};
DE EC=4.2.1.156 {ECO:0000269|PubMed:17649980};
DE EC=4.2.1.42 {ECO:0000269|PubMed:17649980, ECO:0000269|PubMed:29248502};
DE AltName: Full=StTGD {ECO:0000303|PubMed:29248502};
GN OrderedLocusNames=STM3697;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP REGIOCHEMISTRY OF THE REACTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=19883118; DOI=10.1021/bi901731c;
RA Rakus J.F., Kalyanaraman C., Fedorov A.A., Fedorov E.V.,
RA Mills-Groninger F.P., Toro R., Bonanno J., Bain K., Sauder J.M.,
RA Burley S.K., Almo S.C., Jacobson M.P., Gerlt J.A.;
RT "Computation-facilitated assignment of the function in the enolase
RT superfamily: a regiochemically distinct galactarate dehydratase from
RT Oceanobacillus iheyensis.";
RL Biochemistry 48:11546-11558(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=29248502; DOI=10.1016/j.ab.2017.12.015;
RA Easton N.M., Aboushawareb S.A.E., Bearne S.L.;
RT "A continuous assay for L-talarate/galactarate dehydratase using circular
RT dichroism.";
RL Anal. Biochem. 544:80-86(2018).
RN [4] {ECO:0007744|PDB:2PP0, ECO:0007744|PDB:2PP1, ECO:0007744|PDB:2PP3}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-197 IN
RP COMPLEXES WITH AN ANALOG OF THE ENOLATE INTERMEDIATE; L-GLUCARATE AND
RP MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBSTRATE
RP SPECIFICITY, COFACTOR, DISRUPTION PHENOTYPE, SUBUNIT, REACTION MECHANISM,
RP ACTIVE SITES, AND MUTAGENESIS OF LYS-197 AND HIS-328.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=17649980; DOI=10.1021/bi7008882;
RA Yew W.S., Fedorov A.A., Fedorov E.V., Almo S.C., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily: L-
RT talarate/galactarate dehydratase from Salmonella typhimurium LT2.";
RL Biochemistry 46:9564-9577(2007).
CC -!- FUNCTION: Catalyzes the efficient dehydration of both L-talarate (also
CC called L-altrarate) and galactarate to 5-keto-4-deoxy-D-glucarate (5-
CC KDG) (PubMed:17649980, PubMed:29248502). Also catalyzes the
CC epimerization of L-talarate to galactarate; epimerization occurs in
CC competition with dehydration. Is required for the utilization of L-
CC talarate as a carbon source. Also functions in galactarate utilization.
CC Is not active on other acid sugars (PubMed:17649980).
CC {ECO:0000269|PubMed:17649980, ECO:0000269|PubMed:29248502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-altrarate = 5-dehydro-4-deoxy-D-glucarate + H2O;
CC Xref=Rhea:RHEA:44028, ChEBI:CHEBI:15377, ChEBI:CHEBI:37547,
CC ChEBI:CHEBI:42819; EC=4.2.1.156;
CC Evidence={ECO:0000269|PubMed:17649980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44029;
CC Evidence={ECO:0000269|PubMed:17649980};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactarate = 5-dehydro-4-deoxy-D-glucarate + H2O;
CC Xref=Rhea:RHEA:16005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16537,
CC ChEBI:CHEBI:42819; EC=4.2.1.42;
CC Evidence={ECO:0000269|PubMed:17649980, ECO:0000269|PubMed:29248502};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16006;
CC Evidence={ECO:0000269|PubMed:17649980, ECO:0000269|PubMed:29248502};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-altrarate = galactarate; Xref=Rhea:RHEA:64172,
CC ChEBI:CHEBI:16537, ChEBI:CHEBI:37547;
CC Evidence={ECO:0000269|PubMed:17649980};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17649980};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17649980};
CC -!- ACTIVITY REGULATION: Competitively inhibited by tartronate.
CC {ECO:0000269|PubMed:29248502}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for L-talarate {ECO:0000269|PubMed:17649980};
CC KM=330 uM for galactarate {ECO:0000269|PubMed:17649980};
CC KM=380 uM for galactarate {ECO:0000269|PubMed:29248502};
CC Note=kcat is 2.1 sec(-1) with L-talarate as substrate
CC (PubMed:17649980). kcat is 3.6 sec(-1) with galactarate as substrate
CC (PubMed:17649980). kcat is 4.8 sec(-1) with galactarate as substrate
CC (PubMed:29248502). {ECO:0000269|PubMed:17649980,
CC ECO:0000269|PubMed:29248502};
CC -!- SUBUNIT: Homooctamer; tetramer of dimers.
CC {ECO:0000305|PubMed:17649980}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC on L-talarate as carbon source, and are impaired in the ability to
CC utilize galactarate as carbon source. {ECO:0000269|PubMed:17649980}.
CC -!- MISCELLANEOUS: The enzyme product is the enantiomer of the product
CC obtained in the galactarate dehydratase reaction catalyzed by OB2843;
CC the enzymes thus differ in their regiochemistry of dehydration.
CC {ECO:0000305|PubMed:19883118}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; AE006468; AAL22556.1; -; Genomic_DNA.
DR RefSeq; NP_462597.1; NC_003197.2.
DR RefSeq; WP_001218249.1; NC_003197.2.
DR PDB; 2PP0; X-ray; 2.20 A; A/B/C=1-398.
DR PDB; 2PP1; X-ray; 2.20 A; A/B/C/D/E/F=1-398.
DR PDB; 2PP3; X-ray; 2.20 A; A/B/C=1-398.
DR PDBsum; 2PP0; -.
DR PDBsum; 2PP1; -.
DR PDBsum; 2PP3; -.
DR AlphaFoldDB; Q8ZL58; -.
DR SMR; Q8ZL58; -.
DR STRING; 99287.STM3697; -.
DR PaxDb; Q8ZL58; -.
DR EnsemblBacteria; AAL22556; AAL22556; STM3697.
DR GeneID; 1255221; -.
DR KEGG; stm:STM3697; -.
DR PATRIC; fig|99287.12.peg.3910; -.
DR HOGENOM; CLU_030273_3_1_6; -.
DR OMA; WVEHFDW; -.
DR PhylomeDB; Q8ZL58; -.
DR BioCyc; SENT99287:STM3697-MON; -.
DR BRENDA; 4.2.1.156; 5542.
DR BRENDA; 4.2.1.42; 5542.
DR EvolutionaryTrace; Q8ZL58; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0008867; F:galactarate dehydratase activity; IDA:CACAO.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:1990594; F:L-altrarate dehydratase activity; IDA:CACAO.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR GO; GO:0046392; P:galactarate catabolic process; IMP:CACAO.
DR GO; GO:1903663; P:L-altrarate catabolic process; IMP:CACAO.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR033978; L-talarate_dehydratase.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00134; L-talarate/galactarate_dehydra; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..398
FT /note="L-talarate/galactarate dehydratase"
FT /id="PRO_0000429330"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:17649980"
FT ACT_SITE 328
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 46..48
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17649980"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17649980"
FT SITE 301
FT /note="Increases basicity of active site His"
FT MUTAGEN 197
FT /note="K->A: Loss of dehydration activity on both L-
FT talarate and galactarate and loss of epimerization
FT activity."
FT /evidence="ECO:0000269|PubMed:17649980"
FT MUTAGEN 328
FT /note="H->N,A: Loss of dehydration activity on both L-
FT talarate and galactarate and loss of epimerization
FT activity."
FT /evidence="ECO:0000269|PubMed:17649980"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 28..44
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 57..69
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:2PP0"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:2PP0"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:2PP0"
SQ SEQUENCE 398 AA; 44027 MW; 3AE71E6203A1C900 CRC64;
MALSANSDAV TYAKAANTRT AAETGDRIEW VKLSLAFLPL ATPVSDAKVL TGRQKPLTEV
AIIIAEIRSR DGFEGVGFSY SKRAGGQGIY AHAKEIADNL LGEDPNDIDK IYTKLLWAGA
SVGRSGMAVQ AISPIDIALW DMKAKRAGLP LAKLLGAHRD SVQCYNTSGG FLHTPLDQVL
KNVVISRENG IGGIKLKVGQ PNCAEDIRRL TAVREALGDE FPLMVDANQQ WDRETAIRMG
RKMEQFNLIW IEEPLDAYDI EGHAQLAAAL DTPIATGEML TSFREHEQLI LGNASDFVQP
DAPRVGGISP FLKIMDLAAK HGRKLAPHFA MEVHLHLSAA YPLEPWLEHF EWLNPLFNEQ
LELRDGRMWI SDRHGLGFTL SEQARRWTQL TCEFGKRP
