ID   CHMO_ACISP              Reviewed;         543 AA.
AC   P12015;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cyclohexanone 1,2-monooxygenase;
DE            EC=1.14.13.22;
OS   Acinetobacter sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=NCIB 9871;
RX   PubMed=3338974; DOI=10.1128/jb.170.2.781-789.1988;
RA   Chen Y.-C.J., Peoples O.P., Walsh C.T.;
RT   "Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence
RT   determination.";
RL   J. Bacteriol. 170:781-789(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclohexanone + H(+) + NADPH + O2 = H2O + hexano-6-lactone +
CC         NADP(+); Xref=Rhea:RHEA:24068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17854, ChEBI:CHEBI:17915,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.22;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; M19029; AAA21892.1; -; Genomic_DNA.
DR   PIR; A28550; A28550.
DR   AlphaFoldDB; P12015; -.
DR   SMR; P12015; -.
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   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD;
KW   Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3338974"
FT   CHAIN           2..543
FT                   /note="Cyclohexanone 1,2-monooxygenase"
FT                   /id="PRO_0000186455"
FT   BINDING         16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   SITE            327
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   543 AA;  60892 MW;  4FBF0915C7BD25D2 CRC64;
     MSQKMDFDAI VIGGGFGGLY AVKKLRDELE LKVQAFDKAT DVAGTWYWNR YPGALTDTET
     HLYCYSWDKE LLQSLEIKKK YVQGPDVRKY LQQVAEKHDL KKSYQFNTAV QSAHYNEADA
     LWEVTTEYGD KYTARFLITA LGLLSAPNLP NIKGINQFKG ELHHTSRWPD DVSFEGKRVG
     VIGTGSTGVQ VITAVAPLAK HLTVFQRSAQ YSVPIGNDPL SEEDVKKIKD NYDKSLGWCM
     NSALAFALNE STVPAMSVSA EERKAVFEKA WQTGGGFRFM FETFGDIATN MEANIEAQNF
     IKGKIAEIVK DPAIAQKLMP QDLYAKRPLC DSGYYNTFNR DNVRLEDVKA NPIVEITENG
     VKLENGDFVE LDMLICATGF DAVDGNYVRM DIQGKNGLAM KDYWKEGPSS YMGVTVNNYP
     NMFMVLGPNG PFTNLPPSIE SQVEWISDTI QYTVENNVES IEATKEAEEQ WTQTCANIAE
     MTLFPKAQSW IFGANIPGKK NTVYFYLGGL KEYRTCASNC KNHAYEGFDI QLQRSDIKQP
     ANA