ID Q13I37_PARXL Unreviewed; 547 AA.
AC Q13I37;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:ABE36252.1};
GN ORFNames=Bxe_C0337 {ECO:0000313|EMBL:ABE36252.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36252.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE36252.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE36252.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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}.
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DR EMBL; CP000272; ABE36252.1; -; Genomic_DNA.
DR RefSeq; WP_011493512.1; NZ_CP008761.1.
DR AlphaFoldDB; Q13I37; -.
DR STRING; 266265.Bxe_C0337; -.
DR KEGG; bxb:DR64_8098; -.
DR KEGG; bxe:Bxe_C0337; -.
DR PATRIC; fig|266265.5.peg.8111; -.
DR eggNOG; COG2072; Bacteria.
DR OrthoDB; 9766402at2; -.
DR Proteomes; UP000001817; Chromosome 3.
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; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-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:ABE36252.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 547 AA; 61917 MW; E490874E3F13833A CRC64;
MLKKIETKTF DVVVVGAGIT GIYQVYVLRN MGFTVQGYEG GEDVGGTWYW NRYPGCRLDT
ESYAYGYFAL TGIIPEWKWS ERFAGQPEML RYVNHAADRM DVRRSYQFST RVVRADWNDS
TNMWDLELSD QGRVSCRYLI SAVGPLSATR MPNIAGIERF EGESFHTSRW PRDPDDPRGA
RKIDFAGKRV GVIGTGATGV QIIPIVARTA AELFVFQRSP NWCTPLGNHP ISDQEMEKLQ
AAYEEILAFV KSTPTAFPYN RHPKKASETT AEERQALFES LYSMPGYGIW LSGYRDVLLS
RTSNGYLAEF IAGKIRQRVK DPVIAGKLIP RDHPFGTKRV PMETNYYETY NRPNVHLVDV
RETPITCVTP RGLQVGSKHY DLDIIIYATG FDAVTGSFDQ IDIRGKDGLS LKETWQDGPL
TYLGLQTRGF PNFFTLVGPH NGATFCNVGV CGALQVEWVS EMLGYMREHD LTYSEASHVA
QEDWTRQVYE DFSRTLLTEA DAWWIKVKVH PDGTRERRAL VHVSGGPEYR EICDEVAADG
YAGFELH
//
