ID   A0A2J5HS40_9EURO        Unreviewed;       485 AA.
AC   A0A2J5HS40;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   SubName: Full=Putative flavin dependent monooxygenase {ECO:0000313|EMBL:PLN80121.1};
GN   ORFNames=BDW42DRAFT_171581 {ECO:0000313|EMBL:PLN80121.1};
OS   Aspergillus taichungensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN80121.1, ECO:0000313|Proteomes:UP000235023};
RN   [1] {ECO:0000313|Proteomes:UP000235023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA   Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA   Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA   LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA   Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA   Cantor M.N., Hua S.X.;
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; KZ559551; PLN80121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J5HS40; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000235023; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PIRSF; PIRSF000332; FMO; 3.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:PLN80121.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   485 AA;  54838 MW;  E85DEAE6299815F1 CRC64;
     MSLSIPVRRI AVIGAGPSGL AAVKYLLAEK CFEKIDVYER RAQPGGVWNY CPATIKQLMK
     TPVPQTTPDV GLEEPIWHPK GNAKDQMEPT FVSPIYSTLD TNIPKELMAY GEKAFPADSQ
     ELPKYTTVKQ YLDEYAAEVK HLVQFETQVL DVRLKGKDSQ TWALTTRNLQ TRAERTETYD
     AVIVASGHFD VPYLPDIVGI KDWDVAYPGA ISHSKLYDSP DPFHGKKVVV VGSSASGLDI
     GNQINKVSKD KVLASHRAMP LPTTTDKIYV PEIVEFLSPA THDRAVRFAD GRVEAEIDSV
     LFCTGYFYSF PFLSSLDPPV VTDGRRVENI YQHIFYAPNP TLIFPVLPQR IIPFPLAENQ
     AAVFSRVLSG RLALPSYAEM KEWETSTIEQ RGSGTPFHVM PFPLDVDYMN MLNDWASKAE
     PRPGLSDDQN GKQCNRWGEK NKWIRQLTPE IRRVFFEKGE ERRTIRSLEE LGYDFEQWQK
     EQATL
//