ID   A0A2S8LHM3_9MYCO        Unreviewed;       494 AA.
AC   A0A2S8LHM3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Monooxygenase {ECO:0000313|EMBL:PQP51024.1};
GN   ORFNames=C6A82_08055 {ECO:0000313|EMBL:PQP51024.1};
OS   Mycobacterium sp. ITM-2016-00318.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=2099693 {ECO:0000313|EMBL:PQP51024.1};
RN   [1] {ECO:0000313|EMBL:PQP51024.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITM-2016-00318 {ECO:0000313|EMBL:PQP51024.1};
RA   Meehan C.J., Cogneau S., Rigouts L., Shojaei H., Azadi D.;
RT   "Bioremediation-capable novel species from Iranian environmental samples:
RT   Mycobacterium khaydaluicum sp. nov., Mycobacterium meyganicum sp. nov.,
RT   Mycobacterium omidicum sp. nov., Mycobacterium seymaricum sp. nov.,
RT   Mycobacterium austroafricanum subspecies dezhpoolicum subsp. nov.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:PQP51024.1}.
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DR   EMBL; PUTV01001218; PQP51024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8LHM3; -.
DR   OrthoDB; 5168853at2; -.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:PQP51024.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   494 AA;  55118 MW;  D4DC8492B2612D0A CRC64;
     MKPVPDHDTV IVGAGFSGIG TAILLDKAGL GDYLLIEAAD GCGGTWHWNT YPGIAVDIPS
     FSYQFSFEQS ADWTRTYARG RELKDYAEHC VDKYGLRPRI RFNTKVAAAV FDDEVDLWRI
     ETDSGETLTA RFLVNAGGVL TTPQLPDIDG VDSFAGVTMH TARWDHGQDL TGKRVAILGT
     GASAVQVIPE IAPIVDHLAV FQRTPIWCFP KADLALPPIA RQAMRLPGGK ALQRLLSQAY
     VELTFPLAAQ YFTVNPMAKR APDLGRAFLR KEVRDPVVRD KLTPRYAVGC KRPGFHNTYL
     STFNRDNVSL VTEPIDKITG SGVATTDGQV HEVDVLILAT GFKVLDPDGV LTYSVAGPAG
     RTLSEYWTQN RLQAYEGVSI PGFPNFFTVF GPYGYVGSSY FALIEAQSHH IVRCLEHAQR
     RGADRVEVKQ DANDRYFDEM MRKRHRQIFW QDSCSLANSY YFDKNGDVPL RPATTMHAYW
     RSRRFPLDDY EFSA
//