ID   A0A319E716_ASPSB        Unreviewed;       468 AA.
AC   A0A319E716;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 8.
DE   SubName: Full=Putative FAD dependent oxidoreductase {ECO:0000313|EMBL:PYI02388.1};
GN   ORFNames=BO78DRAFT_377125 {ECO:0000313|EMBL:PYI02388.1};
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:PYI02388.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI02388.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI02388.1,
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=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00043981}.
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DR   EMBL; KZ826396; PYI02388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319E716; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   Gene3D; 1.10.405.20; -; 1.
DR   Gene3D; 3.30.70.1990; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR42923:SF26; FMN REDUCTASE LOT6, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06600)-RELATED; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..468
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016390753"
SQ   SEQUENCE   468 AA;  50831 MW;  CDB71C6FBBA7C09F CRC64;
     MLTTFFCLAN VAGALAAAVH TRDQFDSSAY AAEDVIEREF AIIGGGASGT YAAVSLADQN
     KTFTLVEVSD RLGGNTRTFH DPSTGAMVDY GVQIHLDCDI VRDFFARLNS SLASMPLSQY
     GNPKYYDFTK QVALPNHTAG NVESDYVTTL DEYPYVENLI DLPESVPADL LLTWPDFAKK
     HNLSLGSTEG GLAWPATPGD PLNTTALAIF NDGNHVELAE FTGDGLHNAN NDNSLIYVNA
     LAELKADVLL NSKIIAGQRG LNRTSGVQLV ADTPSGKRLI KAKQLIIAMP PLLDNTKYFG
     LDEQEEAILS KLSGKHYYGG VVNNTGLEDG IAYTNVGVDR PYNVASLPGV VEIASTGSAG
     YQFYWYNTIE ATTQAEVEDA TRSTIQWLQT QSNATTVEPN FVAYHDFSPF HLSPPTEDIA
     DGWYTKMKGL QGYRNTWYIS SLFVVGSTQL WNSTQNILPD IISAAAQS
//