ID   H6BTE0_EXODN            Unreviewed;       558 AA.
AC   H6BTE0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:EHY54337.1};
GN   ORFNames=HMPREF1120_02507 {ECO:0000313|EMBL:EHY54337.1};
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:EHY54337.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY54337.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY54337.1};
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; JH226131; EHY54337.1; -; Genomic_DNA.
DR   RefSeq; XP_009154798.1; XM_009156550.1.
DR   AlphaFoldDB; H6BTE0; -.
DR   GeneID; 20307146; -.
DR   VEuPathDB; FungiDB:HMPREF1120_02507; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006937_8_1_1; -.
DR   InParanoid; H6BTE0; -.
DR   OMA; SMPNMFM; -.
DR   OrthoDB; 2041362at2759; -.
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; PTHR43098:SF5; DUAL-FUNCTIONAL MONOOXYGENASE_METHYLTRANSFERASE PSOF; 1.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:EHY54337.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304}.
SQ   SEQUENCE   558 AA;  63320 MW;  57B6F13A073BB814 CRC64;
     MGSIGIQQEQ LYDVLIIGAG LSGLCSLYHI RQRFPDWRVK ILEAGDDVGG TWYWNRYPGA
     RFDSESVSYG FSFDKELLKE WHWKETFSPQ PETLKYIQRV AEKNDLRKDI QFNTRVKSAV
     WDDATHTWVL MDEAGNVYRT TFFVSCLGFL SLPTLPKIPG LSSFEGEKFH TAQWPKDFDL
     KRDFANKRIG VIGTGATGIQ TITEIAKEPS IKSLTVFQRT ANWSAPLRNS PITEEQMEEL
     KAKYDEIFAR CAATPMGFLH KADPRKSAEV SPEERRKLWE EIYAQPGFTK WLGAFSDTFT
     DREANKLYSD FMAEKIRERV KDPKVAEKLI PKNHGFGTRR VPLESGYFES YNKENVHLVD
     LQETPIREVT PKGIVTSDGK EHELDVLIFA TGFNAITGAF SAIEWSVKGG RPLIGTSETE
     KGRNAVWVDH RPKTFLGITV PSVPNMFMVL GPHQPFGNAT RNIEHAVQVV TDLLQYCKDN
     GYTSVEPSQE AVEQWTEHVV ECSKGSLANE VDSWMTGVNT NVAGKQTRSV ARYGGSAIEF
     RRRCRECKEH NWEGLVFA
//