(data stored in SCRATCH zone)

SWISSPROT: Q13I37_PARXL

ID   Q13I37_PARXL            Unreviewed;       547 AA.
AC   Q13I37;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 78.
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; Proteobacteria; 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.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR   EMBL; CP000272; ABE36252.1; -; Genomic_DNA.
DR   RefSeq; WP_011493512.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0337; -.
DR   EnsemblBacteria; ABE36252; ABE36252; Bxe_C0337.
DR   GeneID; 4009851; -.
DR   KEGG; bxb:DR64_8098; -.
DR   KEGG; bxe:Bxe_C0337; -.
DR   PATRIC; fig|266265.5.peg.8111; -.
DR   eggNOG; ENOG4105F95; Bacteria.
DR   eggNOG; COG2072; LUCA.
DR   HOGENOM; HOG000204545; -.
DR   KO; K21730; -.
DR   OMA; HQPFGNA; -.
DR   OrthoDB; 630753at2; -.
DR   BioCyc; BXEN266265:BXE_RS38315-MONOMER; -.
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; -; 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   4: Predicted;
DR   PRODOM; Q13I37.
DR   SWISS-2DPAGE; Q13I37.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Monooxygenase {ECO:0000313|EMBL:ABE36252.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE36252.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
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
//

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