ID   A0A317WUW2_9EURO        Unreviewed;       480 AA.
AC   A0A317WUW2;
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=FAD dependent oxidoreductase {ECO:0000313|EMBL:PWY90214.1};
GN   ORFNames=BO70DRAFT_415770 {ECO:0000313|EMBL:PWY90214.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY90214.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY90214.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY90214.1,
RC   ECO:0000313|Proteomes:UP000247233};
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 (DEC-2016) 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}.
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:PWY90214.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MSFL01000003; PWY90214.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WUW2; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_415770; -.
DR   OrthoDB; 1771364at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR002937; Amino_oxidase.
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; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..480
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016438563"
FT   DOMAIN          49..455
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   480 AA;  52608 MW;  7009A1AC1DBB825B CRC64;
     MTVPTARLFF RFLFLSLFLA PLCPSHVTSQ ARPPETISRD VCIIGGGASG VYTAMRLRQQ
     NISVVVIEAK GRLGGHTNTY IDPGSGTPID FGVALFQDSS ETVDFFAQLN VSLSRSMPVG
     GILQRIDFRT GESVAPNPGN ASEALARYTA VLQRHPYLAE GWNLPDDIPE DLLMSFGQLA
     KKYDLGPVME TISLYTQGVR SWLDYPAVYL LKFMSLDLVT SLRQGFLQAS GHGSSELYQA
     ALRLLGGDVL LRSVVVAASR TGDEGQGQGQ GQGHELTVQT EDEQVVTVQA ALTILAVPPK
     GPVLEGFDLD AHEATLFGHF LNGHYYVGLV RVPHYPSGLQ LLNRGAHTPY GLPRLPCTFS
     VAATAVPDIV TVSYVSEEPR SAEEVQQAVG EDILRVLGRE RQDDEEPRFV AFADHSPFEM
     SVSREAIEGR FYDRLNGLQG HRNTFYVGAT WEYPGSSPIW RAVDRLLPAI IRRLEGFQGR
//