DGOD_SALEP
ID DGOD_SALEP Reviewed; 382 AA.
AC B5QUN9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-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=SEN3644;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(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; AM933172; CAR35220.1; -; Genomic_DNA.
DR RefSeq; WP_000704735.1; NC_011294.1.
DR AlphaFoldDB; B5QUN9; -.
DR SMR; B5QUN9; -.
DR KEGG; set:SEN3644; -.
DR HOGENOM; CLU_030273_3_2_6; -.
DR OMA; PRWCFLK; -.
DR UniPathway; UPA00081; UER00518.
DR Proteomes; UP000000613; 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_1000140387"
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
