ID   DGOD1_ECOSM             Reviewed;         382 AA.
AC   B1LPS5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=D-galactonate dehydratase 1 {ECO:0000255|HAMAP-Rule:MF_01289};
DE            Short=GalD 1 {ECO:0000255|HAMAP-Rule:MF_01289};
DE            EC=4.2.1.6 {ECO:0000255|HAMAP-Rule:MF_01289};
GN   Name=dgoD1 {ECO:0000255|HAMAP-Rule:MF_01289};
GN   OrderedLocusNames=EcSMS35_1095;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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; CP000970; ACB16890.1; -; Genomic_DNA.
DR   RefSeq; WP_000705006.1; NC_010498.1.
DR   AlphaFoldDB; B1LPS5; -.
DR   SMR; B1LPS5; -.
DR   EnsemblBacteria; ACB16890; ACB16890; EcSMS35_1095.
DR   KEGG; ecm:EcSMS35_1095; -.
DR   HOGENOM; CLU_030273_3_2_6; -.
DR   OMA; EYMRHTE; -.
DR   UniPathway; UPA00081; UER00518.
DR   Proteomes; UP000007011; 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 1"
FT                   /id="PRO_0000352624"
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;  42550 MW;  BCDE4A9A32777A85 CRC64;
     MKITKITTYR LPPRWMFLKI ETDEGVVGWG EPVIEGRART VEAAVHELGD YLIGQDPSRI
     NDLWQVMYRA GFYRGGPILM SAIAGIDQAL WDIKGKVLNS PVWQLMGGLV RDKIKAYSWV
     GGDRPANVID GIKILREIGF 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