ID Q0SCL2_RHOJR Unreviewed; 498 AA.
AC Q0SCL2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Flavin binding monooxygenase {ECO:0000313|EMBL:ABG94724.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:ABG94724.1};
GN OrderedLocusNames=RHA1_ro02919 {ECO:0000313|EMBL:ABG94724.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94724.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(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; CP000431; ABG94724.1; -; Genomic_DNA.
DR RefSeq; WP_011595598.1; NC_008268.1.
DR AlphaFoldDB; Q0SCL2; -.
DR KEGG; rha:RHA1_ro02919; -.
DR PATRIC; fig|101510.16.peg.2951; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_032067_2_0_11; -.
DR OrthoDB; 5168853at2; -.
DR Proteomes; UP000008710; Chromosome.
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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43872; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR PANTHER; PTHR43872:SF1; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:ABG94724.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABG94724.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
SQ SEQUENCE 498 AA; 55840 MW; CF022BE851363907 CRC64;
MSHTETAAET TGAKTPVEHV DVLIIGAGLS GIGAAYHLQD NFPRRTYAIL ESRESIGGTW
DLFRYPGIRS DSDMYTLGYR FKPWSGEKSI ADGPSILEYV KDTAAEHGID RNIRFRHKVV
RAEWSTADSH WTVDAERTDT GETVRLTADF LMSCSGYYRY DEGYTPEFPG LDRFGGRVVH
PQQWPEDLDY EGKRVVIIGS GATAVTLAPS MAADAAHVTM LQRSPTYIIS MPAKDKLANK
LRRHLPAKLA YGLTRLKNAS VATAIYQLCQ RYPEFMKGRI RQLQEKWLPK GYDIDTHFTP
RYNPWDQRLC LVPNGDLFRA IRNDEVSIVT DHIDTFTETG ITLKSGEELH ADVVVTATGL
NLLAFGGMTL AVDGHDIDLT ETMAYKGMML SGVPNFAFVI GYTNASWTLK ADLVCEYVCR
LLAHMDANGF TQCAPERDSS VEEEPFLDFA AGYVLRSVES FPKQGSKAPW RLRMNYFRDL
VALRHGKILD DAMTFSRP
//
