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Database: UniProt
Entry: A0A162J5N8_CORDF
LinkDB: A0A162J5N8_CORDF
Original site: A0A162J5N8_CORDF 
ID   A0A162J5N8_CORDF        Unreviewed;       381 AA.
AC   A0A162J5N8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Galactonate dehydratase {ECO:0000313|EMBL:OAA64092.1};
GN   ORFNames=LEL_10612 {ECO:0000313|EMBL:OAA64092.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA64092.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA64092.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA64092.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OAA64092.1}.
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DR   EMBL; AZHF01000015; OAA64092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162J5N8; -.
DR   STRING; 1081108.A0A162J5N8; -.
DR   OrthoDB; 1691455at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT   DOMAIN          126..228
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   381 AA;  41985 MW;  E7C5C393973CC7B8 CRC64;
     MGKIAEIKYF RVPPRWLFVK ITDDAGNIGW GEASLEGHTQ AVEGCLDAWI AQYVGFEADD
     IEHIWQLSWR KTFYRGGPVF MSALSGLDIA LWDLKARKLS VPIYDLLGGK LRSKIKVYAW
     IGGDRPQDVE TAALTRKSQG FTAVKMNGTD DLGWLDSPSA LDSCVERVRT VRALGMDVGV
     DFHGRAHRPM SKQLAAALTP HRPMFIEEPL LPEHVEGYKA LAGLTTIPIA LGERLHSRWD
     VKPFLEGNCV DILQPDTCHV GGISELRRIA AMAEAYDVPI APHCPLGPIA LAACIQVDAA
     TPNFAIQEMS LGIHYNVGGY DLLTYIKNPK IWDVDNGFVN LTTGPGLGIE IDEERVMEAS
     RNAKPWISPG FTGPGGELRE W
//
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