ID   A0A319E8E1_ASPSB        Unreviewed;       383 AA.
AC   A0A319E8E1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Enolase C-terminal domain-like protein {ECO:0000313|EMBL:PYI06356.1};
GN   ORFNames=BO78DRAFT_407502 {ECO:0000313|EMBL:PYI06356.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI06356.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI06356.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI06356.1,
RC   ECO:0000313|Proteomes:UP000248423};
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; KZ826350; PYI06356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319E8E1; -.
DR   STRING; 1448318.A0A319E8E1; -.
DR   Proteomes; UP000248423; 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:UP000248423}.
FT   DOMAIN          126..228
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   383 AA;  42551 MW;  6A719B24AD7A0042 CRC64;
     MVKIKSIEYF RVPPRWLFVK IVDEEGQCGW GESTLEGHTE AVEGTLNALC KRFQGYEADD
     IEHIWQMAWR LGFYRGGPVF MSAISGIDIA LWDLKGRRLG VPIYQLLGGK VRNKLSVYAW
     IGGDRPSDVE AAGKARLAQG FKAIKMNATE DVNWLDSPRA LDSSVERLKA VKALGLDAAL
     DFHGRLHKPM AKQLAKALEP HRPLFLEEPL LSEHPETIKQ LSDQVSCPIA LGERLYSRWD
     VKRFLEDASV DILQPDIAHC GGISELRRIA SMAETYDVAI APHCPLGPIA LAACMQVDLA
     TPNFVIQEMS LGMHYNTEAG EYDITSYVKD SSVFAVKDGY VDALTAPGLG IEVNEDLVRQ
     LAANSEPWPP KEFYGPDGGI REW
//