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Database: UniProt
Entry: F3MCK4_9BACL
LinkDB: F3MCK4_9BACL
Original site: F3MCK4_9BACL 
ID   F3MCK4_9BACL            Unreviewed;       382 AA.
AC   F3MCK4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=D-galactonate dehydratase {ECO:0000313|EMBL:EGG34945.1};
DE            EC=4.2.1.6 {ECO:0000313|EMBL:EGG34945.1};
GN   Name=dgoD {ECO:0000313|EMBL:EGG34945.1};
GN   ORFNames=HMPREF9412_4144 {ECO:0000313|EMBL:EGG34945.1};
OS   Paenibacillus sp. HGF5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG34945.1, ECO:0000313|Proteomes:UP000004272};
RN   [1] {ECO:0000313|EMBL:EGG34945.1, ECO:0000313|Proteomes:UP000004272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGF5 {ECO:0000313|EMBL:EGG34945.1,
RC   ECO:0000313|Proteomes:UP000004272};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000256|ARBA:ARBA00010339}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGG34945.1}.
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DR   EMBL; AEXS01000119; EGG34945.1; -; Genomic_DNA.
DR   RefSeq; WP_009593299.1; NZ_AEXS01000119.1.
DR   AlphaFoldDB; F3MCK4; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000004272; Unassembled WGS sequence.
DR   GO; GO:0008869; F:galactonate dehydratase activity; IEA:UniProtKB-EC.
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; SFLDS00001; Enolase; 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   Lyase {ECO:0000313|EMBL:EGG34945.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          125..230
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   382 AA;  42788 MW;  6858916620B4F6E7 CRC64;
     MKITGYELFL VPPRWLFLKM ETDEGIIGWG EPVIEGKART VGTAVEELME NLIGKDPLRI
     EDHWNLMYRS GFYRGGPILM SAISGIDQAL WDIKGKYYNA PVHQLLGGKA RESIKVYSWI
     GGDRPSDVGK SAKEVVSRGF TAVKMNGTEE LQYVDSYEKI DQVIERIAAV RDAVGPYVGI
     GIDFHGRVHK PMAKILAKEL EPFRPMFIEE PVLPENNEAL RDIANHVAIP IATGERMFSK
     WEFKRILMDG YVDIIQPDLS HAGGITECKK IISMAEAFDV AAAPHCPLGP IALASCLQVD
     ATCHNAFIQE QSLGIHYNQG SDLLDYIVDN LVFEYENGYV KIPEGPGLGI EINEDHVRKM
     ADIGHNWRNP VWRHTDGSIA EW
//
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