ID   DGOD_SALNS              Reviewed;         382 AA.
AC   B4SY97;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=D-galactonate dehydratase {ECO:0000255|HAMAP-Rule:MF_01289};
DE            Short=GalD {ECO:0000255|HAMAP-Rule:MF_01289};
DE            EC=4.2.1.6 {ECO:0000255|HAMAP-Rule:MF_01289};
GN   Name=dgoD {ECO:0000255|HAMAP-Rule:MF_01289};
GN   OrderedLocusNames=SNSL254_A4112;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-
CC       D-galactonate. {ECO:0000255|HAMAP-Rule:MF_01289}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O;
CC         Xref=Rhea:RHEA:18649, ChEBI:CHEBI:12931, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57989; EC=4.2.1.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01289};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01289};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01289};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-galactonate degradation; D-
CC       glyceraldehyde 3-phosphate and pyruvate from D-galactonate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_01289}.
CC   -!- MISCELLANEOUS: Reaction proceeds via an anti dehydration.
CC       {ECO:0000255|HAMAP-Rule:MF_01289}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000255|HAMAP-Rule:MF_01289}.
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DR   EMBL; CP001113; ACF61964.1; -; Genomic_DNA.
DR   RefSeq; WP_000704735.1; NZ_CCMR01000001.1.
DR   AlphaFoldDB; B4SY97; -.
DR   SMR; B4SY97; -.
DR   EnsemblBacteria; ACF61964; ACF61964; SNSL254_A4112.
DR   KEGG; see:SNSL254_A4112; -.
DR   HOGENOM; CLU_030273_3_2_6; -.
DR   OMA; PRWCFLK; -.
DR   UniPathway; UPA00081; UER00518.
DR   Proteomes; UP000008824; Chromosome.
DR   GO; GO:0008869; F:galactonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0034194; P:D-galactonate catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03325; D-galactonate_dehydratase; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   HAMAP; MF_01289; Galacton_dehydrat; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR023592; Galactonate_deHydtase.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; PTHR48080; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00003; D-galactonate_dehydratase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..382
FT                   /note="D-galactonate dehydratase"
FT                   /id="PRO_1000140390"
FT   ACT_SITE        185
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        285
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01289"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01289"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01289"
FT   SITE            258
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01289"
FT   SITE            310
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01289"
SQ   SEQUENCE   382 AA;  42379 MW;  51A2D7F9CF9C7DE8 CRC64;
     MKITHITTYR LPPRWMFLKI ETDEGVVGWG EPVIEGRART VEAAVHEFAD YLIGKDPARI
     NDLWQVMYRA GFYRGGPIMM SAIAGIDQAL WDIKGKVLNA PVWQLMGGLV RDKIKAYSWV
     GGDRPADVID GIEKLRGIGF DTFKLNGCEE MGVIDNSRAV DAAVNTVAQI REAFGSEIEF
     GLDFHGRVSA PMAKVLIKEL EPYRPLFIEE PVLAEQAEYY PRLAAQTHIP IAAGERMFSR
     FEFKRVLDAG GLAILQPDLS HAGGITECYK IAGMAEAYDV ALAPHCPLGP IALAACLHID
     FVSRNAVFQE QSMGIHYNKG AELLDFVKNK EDFSMDGGFF KPLTKPGLGV DIDEARVIEL
     SKSAPDWRNP LWRHADGSVA EW