ID   DGOD_XANOM              Reviewed;         382 AA.
AC   Q2P1Q3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; OrderedLocusNames=XOO2769;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE69524.1; -; Genomic_DNA.
DR   RefSeq; WP_011408875.1; NC_007705.1.
DR   AlphaFoldDB; Q2P1Q3; -.
DR   SMR; Q2P1Q3; -.
DR   KEGG; xom:XOO2769; -.
DR   HOGENOM; CLU_030273_3_2_6; -.
DR   OMA; PRWCFLK; -.
DR   UniPathway; UPA00081; UER00518.
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_0000352643"
FT   REGION          361..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  41926 MW;  CCAA636259154835 CRC64;
     MKITRLTTYH AAPRWLFLKV ETDEGITGWG EPVIEGRARS VEAAVHELAG YVVGKDPARI
     NDLWQTMYRA GFYRGGAILM SAIAGIDQAL WDIKGKALGV PVYELLGGLV RDRMKTYRWV
     GGDRPGAIIQ QITDYRALGF DTFKFNGTEE MKLIDSARAV DAAVVKVAEI REAFGNTIDF
     GIDFHGRVGA PMAKALLREL EPFKPLFVEE PVLAEQAEYY PRLAASTSIP LAAGERMFSR
     FEFKNVLCAG GIGMVQPDLS HAGGITECVK IAAIAEAYDV GFAPHCPLGP IALAACLHVD
     FVSHNAVLQE QSIGIHYNEG ADLLDYVINK DDFHCVDGSI AALPKPGLGV EIDEDMLKRA
     NENPPDWRNP VWRHSDGSIA EW