ID   H6C0L0_EXODN            Unreviewed;       509 AA.
AC   H6C0L0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Dimethylaniline monooxygenase (N-oxide forming) {ECO:0000313|EMBL:EHY57252.1};
GN   ORFNames=HMPREF1120_05296 {ECO:0000313|EMBL:EHY57252.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57252.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY57252.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57252.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; JH226133; EHY57252.1; -; Genomic_DNA.
DR   RefSeq; XP_009157713.1; XM_009159465.1.
DR   AlphaFoldDB; H6C0L0; -.
DR   GeneID; 20309935; -.
DR   VEuPathDB; FungiDB:HMPREF1120_05296; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_5_2_1; -.
DR   InParanoid; H6C0L0; -.
DR   OMA; GPCYESL; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000007304; 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; 3.
DR   PIRSF; PIRSF000332; FMO; 3.
DR   PRINTS; PR00419; ADXRDTASE.
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:EHY57252.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304}.
SQ   SEQUENCE   509 AA;  56672 MW;  562B425ACEDA49C8 CRC64;
     MVETHPKRVA VIGAGISGVT SAAHLLKHGL DVTLFERSGV AGGVWHFDER SALEPAYPNE
     TPSRGDYETK PELAYLTPPP EATGDKLEEV EIAHAPPGPC YAGLKNNVST RLMRTSLQAW
     PEGTPDFVSQ KTVEEYVQTI ADAHGVSPVA QYNTRVEEVR KQGTEWYVRT TTLQKSPTSF
     GAPQLAERRW TFDAIVAASG HYHMPRVPDI PGLKDWKREH PDRVWHSKRY RNPAVFKDQN
     ILLIGAGVSS LDIAKESSST ANKIYQSSRG GALDLPANLL PENATRVAGI KEFRLTTAQT
     ADPLKLQPIA GTVVLEDGQE LTDIHSVVLC TGYITSYPFL SHLHADTRSA EEADDSVLVT
     REGEMVHNLH KDIFYIEDPS LAFVGAPYHI ATFSLFDFQA QVVARVLAGK ALLPPKEVMR
     EEYRQRVKTK GLGRNFHSLR GAGEEQRYVA DLVNWMNESA EQLGIEDKMQ GHTEEWHKAN
     IDREEQLKWL RATKTQKKEE EVGKELVSA
//