ID A4TBY9_MYCGI Unreviewed; 453 AA.
AC A4TBY9;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:ABP46208.1};
DE EC=1.14.13.22 {ECO:0000313|EMBL:ABP46208.1};
GN OrderedLocusNames=Mflv_3736 {ECO:0000313|EMBL:ABP46208.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP46208.1};
RN [1] {ECO:0000313|EMBL:ABP46208.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46208.1};
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP46208.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46208.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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DR EMBL; CP000656; ABP46208.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TBY9; -.
DR KEGG; mgi:Mflv_3736; -.
DR eggNOG; COG2072; Bacteria.
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:ABP46208.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABP46208.1}.
SQ SEQUENCE 453 AA; 51114 MW; 2632093099268DEE CRC64;
MVLEHLSRCR SGHSVVPHQF SFEQSTEWSR TYAPGRELKS YADHCFDKYG LRSRTRFATT
VRSAEFDDSA GLWRLAVESG GVQSTVTARF VINAGGALTV PNLPDIPGVD SFAGTTIHTA
RWDHDVDLTG KRVAIIGTGA SAVQVIPEIA PIVARLTVFQ RTPIWCFPKF DVPLSRTARA
MMRLPFGQTL QRFLSQAYVE LTFPLAAQYF TVNPMAKRMS RMGLAYLRRQ VKDPVVREKL
TPRYAVGCKR PGFHNTYLAT FNRDNVELVT EPIDKITGAG VATTDGQLRD ADVLILATGF
KVLDTENVPT YRVTGSGGRS LSRFWEENRL QAYEGVSVPG FPNFFTVFGP YGYVGSSYFA
LIEAQTRHIV RCLAEAGRRG ASRVEVRREA NDRYFAEMMR KRHRQIFWQD SCRLSNSYYF
DQHGDVPLRP ASTLEAHWRS RSFPIDDYEF AVS
//
