ID   A0A395H179_9EURO        Unreviewed;       381 AA.
AC   A0A395H179;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Enolase C-terminal domain-like protein {ECO:0000313|EMBL:RAL01119.1};
GN   ORFNames=BO80DRAFT_355325 {ECO:0000313|EMBL:RAL01119.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL01119.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL01119.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL01119.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; KZ824437; RAL01119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395H179; -.
DR   STRING; 1448316.A0A395H179; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_355325; -.
DR   OrthoDB; 1691455at2759; -.
DR   Proteomes; UP000249402; 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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT   DOMAIN          126..228
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   381 AA;  41890 MW;  6F3E9D379E27CEAB CRC64;
     MAPITQIEYF RVPPRWLFVK VTDSQGNTGW GEASLEGHTE AVEGCLNAFI ERFIGLEAND
     IEHIWQNGYR MGFYRGGPIL MSALSGIDIA LWDLKARRFG VPIYELLGGK VRDRLRVYAW
     IGGDRPGDVE IQARGRISQG FKAVKMNATE DIGWLDSPGA LNASVERLKT VKSLGLDAGV
     DFHGRVHKAM AIQLAHKLAP HEPLFIEEPL LSEHPESVTA LSKLVPIPIA LGERLHSRWD
     VKPFLESASV SILQPDISHV GGISELRRIA VMAEAYDVAL APHCPLGPIA LAANIQVDAV
     SANFAIQEMS LGIHYNHGSA DLETYIKNGD VWTVKDGMLD LPRGPGLGIE LDEDKIRAAT
     VNAKAWRSPC FEGPGGEWRE W
//