ID   DGOD_ECOSE              Reviewed;         382 AA.
AC   B6I3S5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-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}; OrderedLocusNames=ECSE_3978;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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; AP009240; BAG79502.1; -; Genomic_DNA.
DR   RefSeq; WP_000705001.1; NC_011415.1.
DR   AlphaFoldDB; B6I3S5; -.
DR   SMR; B6I3S5; -.
DR   EnsemblBacteria; BAG79502; BAG79502; ECSE_3978.
DR   GeneID; 66672410; -.
DR   KEGG; ecy:ECSE_3978; -.
DR   HOGENOM; CLU_030273_3_2_6; -.
DR   OMA; PRWCFLK; -.
DR   UniPathway; UPA00081; UER00518.
DR   Proteomes; UP000008199; 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_1000140382"
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;  42523 MW;  B38D4E0B95FD7041 CRC64;
     MKITKITTYR LPPRWMFLKI ETDEGVVGWG EPVIEGRART VEAAVHELGD YLIGQDPSRI
     NDLWQVMYRA GFYRGGPILM SAIAGIDQAL WDIKGKVLNA PVWQLMGGLV RDKIKAYSWV
     GGDRPADVID GIKTLREIGF DTFKLNGCEE LGLIDNSRAV DAAVNTVAQI REAFGNQIEF
     GLDFHGRVSA PMAKVLIKEL EPYRPLFIEE PVLAEQAEYY PKLAAQTHIP LAAGERMFSR
     FDFKRVLEAG GISILQPDLS HAGGITECYK IAGMAEAYDV TLAPHCPLGP IALAACLHID
     FVSYNAVLQE QSMGIHYNKG AELLDFVKNK EDFSMVGGFF KPLTKPGLGV EIDEAKVIEF
     SKNAPDWRNP LWRHEDNSVA EW