ID   A0A2S8WT99_9MICC        Unreviewed;       535 AA.
AC   A0A2S8WT99;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:PQZ94757.1};
GN   ORFNames=CQ018_05270 {ECO:0000313|EMBL:PQZ94757.1};
OS   Arthrobacter sp. MYb227.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ94757.1, ECO:0000313|Proteomes:UP000239972};
RN   [1] {ECO:0000313|EMBL:PQZ94757.1, ECO:0000313|Proteomes:UP000239972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb227 {ECO:0000313|EMBL:PQZ94757.1,
RC   ECO:0000313|Proteomes:UP000239972};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PQZ94757.1}.
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DR   EMBL; PCPT01000002; PQZ94757.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8WT99; -.
DR   OrthoDB; 5168853at2; -.
DR   Proteomes; UP000239972; Unassembled WGS sequence.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:PQZ94757.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239972}.
SQ   SEQUENCE   535 AA;  60175 MW;  1F1C9245D996C489 CRC64;
     MALPNDVDVL VVGAGFSGLY MLHKLRGLGL SAVALEKGDG VGGTWYWNRY PGARCDVESP
     YYSYSFDADL EQEWEWTERY PAQPELLKYI NHVADRFELR KDIFLETTAV SAVFDESENL
     WTVTSIGPEG GHVTRARYCI MATGCLSSAR MPNIPGLESF QGQLLHTGMW PHEEIDFTGQ
     RVGVIGTGSS GIQAIPVIAE QAQNLQVFQR TPNFSVPAFN GPIDQQWYRE IKENYPELRE
     RSRHTTMGIP FQRRDQAAID ISEEEREQVF EEHWPKGGFR ISSCFNDLMR NQESNDSLAS
     FVRNKIDQMV HDPKIAQLLK PYDHPVTGKR ICVDTNYYAT YNRDNVELID VKSDPIQEIT
     AHGIQTEDHF FELDTIVVAT GFDAMTGAML HMDIRGRGGA SLREHWEAGA RTYLGLAVAG
     FPNMFTIAGP GSPSVLSNML TSIEQHVEWI SDHLVHLREG GYTSSEAATV AEDEWVDHVR
     ELSEKTLFPS ANSWYLGANV PGKPRVFMPY IGGVGRYRAH CTDIASRDYE GFVLK
//