ID C1D2H9_DEIDV Unreviewed; 382 AA.
AC C1D2H9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Putative galactonate dehydratase {ECO:0000313|EMBL:ACO47618.1};
GN Name=dgoD {ECO:0000313|EMBL:ACO47618.1};
GN OrderedLocusNames=Deide_1p01680 {ECO:0000313|EMBL:ACO47618.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide1 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47618.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47618.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RC PLASMID=pDeide1 {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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DR EMBL; CP001115; ACO47618.1; -; Genomic_DNA.
DR RefSeq; WP_012694741.1; NC_012527.1.
DR AlphaFoldDB; C1D2H9; -.
DR KEGG; ddr:Deide_1p01680; -.
DR HOGENOM; CLU_030273_3_2_0; -.
DR OMA; PRWCFLK; -.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000002208; Plasmid pDeide1.
DR GO; GO:0008869; F:galactonate dehydratase activity; IEA:InterPro.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR GO; GO:0034194; P:D-galactonate catabolic process; IEA:InterPro.
DR CDD; cd03325; D-galactonate_dehydratase; 1.
DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR InterPro; IPR034593; DgoD-like.
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; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080:SF2; D-GALACTONATE DEHYDRATASE; 1.
DR PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00003; D-galactonate_dehydratase; 1.
DR SFLD; SFLDG00179; mandelate_racemase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:ACO47618.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 125..230
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 382 AA; 42166 MW; D948F053B538FDCF CRC64;
MKITRLESFL VPPRWLFLKI ETDEGVSGWG EPVVEGRAHT VQAAVNELAD LIVGRDPGRI
EDLWQLMHRG GFYRGGAVFM SAIAGIDQAL WDIKGKVFGA PVHSLLGGQC RDRMRVYSWI
GGDRPSDVAA AAHAAMSAGF TAIKMNATEE MTYLDVHSKI DSVLNRVQAV RDATTPDFGI
AVDFHGRLHL PMARVLAREL DPMRLMFIEE PVLSENIEAL REIRRVTTTP LALGERLYSR
WEFKAMLHEG LVDVIQPDLS HAGGITECRK IASMAEAYDV ALAPHCPLGP IALAACLQVD
AVAHNAAIQE QSLGIHYNQG SDLLDYVKDK SVFQYADGYV GLPQGPGLGI EVDEDFVRAQ
AATEHRWRNP LWRHADGSVA EW
//