DGOD_XANCP
ID DGOD_XANCP Reviewed; 382 AA.
AC Q8P9V1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=XCC1746;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM41037.1; -; Genomic_DNA.
DR RefSeq; NP_637113.1; NC_003902.1.
DR RefSeq; WP_011036920.1; NC_003902.1.
DR AlphaFoldDB; Q8P9V1; -.
DR SMR; Q8P9V1; -.
DR STRING; 340.xcc-b100_2515; -.
DR EnsemblBacteria; AAM41037; AAM41037; XCC1746.
DR GeneID; 58013700; -.
DR KEGG; xcc:XCC1746; -.
DR PATRIC; fig|190485.4.peg.1861; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_3_2_6; -.
DR OMA; PRWCFLK; -.
DR UniPathway; UPA00081; UER00518.
DR Proteomes; UP000001010; 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; Reference proteome.
FT CHAIN 1..382
FT /note="D-galactonate dehydratase"
FT /id="PRO_0000352639"
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; 41929 MW; D8F0E17E5572A6CE CRC64;
MKITRLTTYH AAPRWLFLKV ETDEGITGWG EPVIEGRARS VEAAVHELAG YVVGKDPARI
NDLWQTMYRA GFYRGGAILM SAIAGIDQAL WDIKGKALGV PVYELLGGLV RDRMKTYRWV
GGDRPGAIIA QINDYRALGF DTFKFNGTEE MKLIDSARAV DAAVVKVAEI RETFGNSIDF
GIDFHGRVGA PMAKALLREL EPFKPLFVEE PVLAEQAEYY PRLAASTCIP LAAGERMFSR
FEFKNVLCAG GIGMVQPDLS HAGGITECVK IAAMAEAYDV GFAPHCPLGP IALAACLHVD
FVSHNAVLQE QSIGIHYNEG ADLLDYVINK EDFHCVDGSI AALPKPGLGV EINEDMLKRA
NENPPDWRNP VWRHADGSIA EW
