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Database: UniProt
Entry: A0A0Q2MND8_MYCGO
LinkDB: A0A0Q2MND8_MYCGO
Original site: A0A0Q2MND8_MYCGO 
ID   A0A0Q2MND8_MYCGO        Unreviewed;       513 AA.
AC   A0A0Q2MND8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Monooxygenase {ECO:0000313|EMBL:KQH81223.1};
GN   ORFNames=AO501_06405 {ECO:0000313|EMBL:KQH81223.1};
OS   Mycobacterium gordonae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH81223.1, ECO:0000313|Proteomes:UP000051677};
RN   [1] {ECO:0000313|EMBL:KQH81223.1, ECO:0000313|Proteomes:UP000051677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH81223.1,
RC   ECO:0000313|Proteomes:UP000051677};
RA   Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA   Chernousova L.;
RT   "Mycobacterium gordonae draft genome assembly.";
RL   Submitted (OCT-2015) 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:KQH81223.1}.
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DR   EMBL; LKTM01000001; KQH81223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q2MND8; -.
DR   STRING; 1778.A9W97_11020; -.
DR   Proteomes; UP000051677; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00368; FADPNR.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Monooxygenase {ECO:0000313|EMBL:KQH81223.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051677};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   513 AA;  56844 MW;  580432764251291E CRC64;
     MRYVLGRIRA AGRRRPSPKV AIIGAGFGGL GAAVALRRAG IDDLVIIEAA DGVGGTWRRN
     SYPGAACDIQ SHLYSFSFAP NKSWSRTYAR QPEILAYLES VADDFDLRRH LMLNTALRSA
     RWDDGAGRWN LQLDRQGSDR DLAVDVVVCA AGLFGSVRLP EIAGLTEFGG ALMHTAQWDH
     DVDLTGKRVA VIGTGASGVQ VIPELARIAG HLTVFQRTPP WMVPKEDRPY SATELAQFRR
     NPLAARRKRW EIWKFQHDNT ATMADDPIVA ARSQFATSFL ERTVPDEQLR RDLTPDYPFR
     CKRVLLGDDF YRALQRHNVT LVTDPVERLT KTSVVTASGA TVDVDAVVLA TGFETSHYLS
     GIDVVGAGGQ NLHQRWGADP TAYLGVAVPG FPNFFMLYGP NTNQGGNSIV YILEAGARLV
     ASAVSRIARR GGFLQVRPEA EQRYNDRLSA DLERSIWTQC DSYFRSPSGR VVTQWPYTEL
     EYARRTWRVR PGDWVHAQAA SPKIAAGRLP NRP
//
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