ID   L8DFR4_9NOCA            Unreviewed;       646 AA.
AC   L8DFR4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative FAD-dependent monooxygenase {ECO:0000313|EMBL:CCQ15604.1};
GN   ORFNames=RHODMAR_2230 {ECO:0000313|EMBL:CCQ15604.1};
OS   Rhodococcus sp. AW25M09.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ15604.1, ECO:0000313|Proteomes:UP000011207};
RN   [1] {ECO:0000313|EMBL:CCQ15604.1, ECO:0000313|Proteomes:UP000011207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ15604.1,
RC   ECO:0000313|Proteomes:UP000011207};
RA   Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA   Smalaas A.O., Altermark B.;
RT   "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT   from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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:CCQ15604.1}.
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DR   EMBL; CAPS01000059; CCQ15604.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8DFR4; -.
DR   STRING; 1268303.RHODMAR_2230; -.
DR   eggNOG; COG2072; Bacteria.
DR   Proteomes; UP000011207; Unassembled WGS sequence.
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:SF5; L-ORNITHINE N(5)-OXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
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:CCQ15604.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   646 AA;  71463 MW;  F1AD0CCB686CC567 CRC64;
     MSTHAATAAE TEGGVNRDRV DRDRLSRALT AANLPTLVAV LYQLTGDRTW LADPYRPTRS
     RGMDNNDTGG FDDAVADRIR SAALDAICAF HEGTPMAVPA PDSEHLVEMI SVAVGEQVPR
     EFGVMVAEDM GFTASDTPVA APNDLSVIVI GAGVSGMLAA IKLHEAGISH VVLEKNSDVG
     GGWFENTYPG AGVDTPSHLY SYSFAPRAWS THFGKRDEVW QYLSDVASEH DLRQRIRFDT
     EVATAEYDAQ RQGWTVRTVD GETLTADVVI TATGQLNRPK VPLIPGLESF DGPIFHTANW
     PADLDLTGKR VAIVGTGASA MQVLPAIASA VGHATVFQRS PQWVSSSDVY FTEMGDDANY
     LMDVVPLYRL WYRTRLAWNF NDRVHSSLQV DPEWEHPQRS INPMNDAHRR VFTRYIEAEL
     EGRPDLIEKS LPDYPPFGKR MLLDNGWYAA LKRDNVTLIA DAVSSITANS VVARDGSETE
     VDVVILATGF ETHKLLTPID VRGRSGESIR NIWGPEDAHA YLGITVPDFP NFFITCGPGT
     VLGHGGSYIT IAECQVRYII DVLNDMVDKR IGAIECKVDV EAEYVRKHDE AHAKMIWSHG
     GMDNWYRNDA GRVVSTLPWR IVDYWEMTRR ADLDDFVTEA RRDEAP
//