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Database: UniProt
Entry: H6BQL2_EXODN
LinkDB: H6BQL2_EXODN
Original site: H6BQL2_EXODN 
ID   H6BQL2_EXODN            Unreviewed;       572 AA.
AC   H6BQL2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:EHY53829.1};
GN   ORFNames=HMPREF1120_02011 {ECO:0000313|EMBL:EHY53829.1};
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:EHY53829.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY53829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53829.1};
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.
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DR   EMBL; JH226131; EHY53829.1; -; Genomic_DNA.
DR   RefSeq; XP_009154290.1; XM_009156042.1.
DR   AlphaFoldDB; H6BQL2; -.
DR   GeneID; 20306650; -.
DR   VEuPathDB; FungiDB:HMPREF1120_02011; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006937_6_2_1; -.
DR   InParanoid; H6BQL2; -.
DR   OMA; FHKTTVW; -.
DR   OrthoDB; 49786at2759; -.
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; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR42877; -; 1.
DR   PANTHER; PTHR42877:SF8; MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:EHY53829.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304}.
SQ   SEQUENCE   572 AA;  65334 MW;  A22F44B369B65D61 CRC64;
     MGSIDMTSES GYHIKNQWHS QPRPIRIVCI GAGAAGLLVA YKLKRNLKLF DLVIYEKNAG
     IGGTWYENRY PGCACDVPAH VYTYSFEPNP DWSAFYASAP EIRQYFERFA ERYDLYPYIR
     TKTRVLSSTW VEDKGVYELQ VQLEDGTIIQ DWCHILINGT GTLSRWKWPD IPGLHDFKGK
     LVHSADWDTS VDWSGKTVAV IGTGSSAIQI VPQVQKTAEK VICFMRSVTW ISPPIAGDVL
     KETKAHSSDP GQSQTNQYFY TEEDKRRFRE HPDELLAYRK KLESQFTGTF DIFIAGSQMS
     KDAQRLMRDE MYRRIGPGHE ELKKNLIPTW APGCRRMTPG EGYLEALVQD NVVTVHKNIA
     KVVPEGLVDS TGQLHRADII VCATGFDVSH KPNFTVTGVN GADMRQEFEP EPYVYLSMAV
     PKFPNYFTIN GARGSWASGT ALNSHEACVD YIVKCISRIQ TENIRALEVK MEPIKQLYEH
     MDEWHKGSVW NDDCKSWYKN NIPGGKPLLW GGSSLHFIKT LQLVRWEHYD FRYFGKNMWE
     FLGNGRVEAE MTNDIDGLAP YIRNEDTPWS VQ
//
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