ID   A1UHY7_MYCSK            Unreviewed;       394 AA.
AC   A1UHY7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:ABL92445.1};
DE            EC=1.14.13.22 {ECO:0000313|EMBL:ABL92445.1};
GN   OrderedLocusNames=Mkms_3251 {ECO:0000313|EMBL:ABL92445.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92445.1};
RN   [1] {ECO:0000313|EMBL:ABL92445.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL92445.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; CP000518; ABL92445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UHY7; -.
DR   STRING; 189918.Mkms_3251; -.
DR   KEGG; mkm:Mkms_3251; -.
DR   HOGENOM; CLU_006937_7_1_11; -.
DR   GO; GO:0018667; F:cyclohexanone monooxygenase activity; IEA:UniProtKB-EC.
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:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
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:0000313|EMBL:ABL92445.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABL92445.1}.
SQ   SEQUENCE   394 AA;  43681 MW;  0E96FAAC2FF9155D CRC64;
     MSNTRGQVPW TLVTNSNETI TCDVVVSAVG QLSLPHVPVI ADADTFQGPR FHSARWDRSV
     SLRGKQVAVI GTGASAIQFV PHIAQEAEHV TLYQRTAPWI LPKWDSRYGV LHDRVSELLP
     MALRLERFAV WLIFELLAVT LVDAKPLSRV LGAIARRHLH RQVASPSLRE QLMPSDAPGC
     KRVLFSNDYY PAIASDRVSL VPKAIAELCD NGVKTVDGEF RPADVVIYGT GFRATDFLAP
     MSVRGSRGVS LAEVWKTQAY AYLGITVPMF PNLFLLYGPN TNVGSGSILY MIESQVRHIA
     TLIKAVAAHP GHAIDVRTES AQRYNTRLRR RLRRSVWALC ASWYRTSSGE IPTNWPGPTL
     VYRLLTRKPH SGDYVLRNVG RLKVGDPAEP SLAD
//