ID A0A098EJU1_9BACL Unreviewed; 382 AA.
AC A0A098EJU1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=D-galactonate dehydratase {ECO:0000313|EMBL:CEG22085.1};
GN Name=dgoD_2 {ECO:0000313|EMBL:CEG22085.1};
GN ORFNames=BN1080_01005 {ECO:0000313|EMBL:CEG22085.1};
OS Planococcus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG22085.1, ECO:0000313|Proteomes:UP000043699};
RN [1] {ECO:0000313|EMBL:CEG22085.1, ECO:0000313|Proteomes:UP000043699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES2 {ECO:0000313|EMBL:CEG22085.1,
RC ECO:0000313|Proteomes:UP000043699};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GalD subfamily. {ECO:0000256|ARBA:ARBA00010339}.
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DR EMBL; CCXS01000001; CEG22085.1; -; Genomic_DNA.
DR RefSeq; WP_052650815.1; NZ_LR698965.1.
DR AlphaFoldDB; A0A098EJU1; -.
DR STRING; 1499687.BN1080_01005; -.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000043699; Unassembled WGS sequence.
DR GO; GO:0008869; F:galactonate dehydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000043699}.
FT DOMAIN 125..230
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 382 AA; 42781 MW; C09DE35E06114082 CRC64;
MKIISYELFQ VPPRWLFLKI ETDEGIIGWG EPVIEGRAST VKACVHELME YLIGKDPLRI
EDHWNMLYRS GFYRGGPILM SAIAGIDQAL WDIKGKYFDA PVYQLLGGAC RDSIKVYSWI
GGDRPADVGL AAQKVVDAGF TAIKMNGTEE LQYIDSYEKI DQTLARVAAV RESVGPYVGI
GIDFHGRVHK PMAKILAKEL EQFRPMFIEE PVLAENNEAL REIAKHTTIP IATGERMFSR
WDFKQILTEG YVDIIQPDLS HAGGITECKK IATMAEAFDV ALAPHCPLGP IALAACLQVD
ATAHNAFIQE QSLGIHYNQG NDLLDYIKDP SVFEYTEGYV KIPQGAGLGI EINEDYVRQQ
SEIGHNWKNP VWRHQDGSIA EW
//
