ID A0A0D0UT78_9ACTN Unreviewed; 439 AA.
AC A0A0D0UT78;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:KIR61972.1};
GN ORFNames=TK50_31580 {ECO:0000313|EMBL:KIR61972.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR61972.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR61972.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR61972.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:KIR61972.1}.
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DR EMBL; JXSX01000003; KIR61972.1; -; Genomic_DNA.
DR RefSeq; WP_043969164.1; NZ_JXSX01000003.1.
DR AlphaFoldDB; A0A0D0UT78; -.
DR PATRIC; fig|47853.6.peg.6619; -.
DR OrthoDB; 5168853at2; -.
DR Proteomes; UP000032254; 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; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
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:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:KIR61972.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000032254};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..439
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038616909"
SQ SEQUENCE 439 AA; 47168 MW; B5F34EEED4103E7A CRC64;
MGQPPRVAVI GAGAAGLATL KALADAGVPA AAFEATDTIG GLWVYGAPDS PAYRTLHLNT
SRTRTQFADH PMPAHWPDYP DHTRVAGYLR DYAHRFGLLD TVRLRHTVVG VTRGPDDRWT
VRTTGPHGTS DVTVAAVVVA NGHNRVPRPP APLPAGDCTA EQLHSHAYRG PEQLAGRRVL
VVGGGNSAMD IAVDASHTAR RTLLSLRRGV WVVPKHLLGR PSDTLNGALA RRLPWRLRQR
ISQTLLTATV GPPTRYGLPA PTHGFLQDHP TLSDGLLSRL THGEIEARPG VAAFHGDQVE
FTDGRVDTVD LVVWCTGYRV EVPFLDPGLL GTGPDTLPLY RHVFHLDAPG LAFVGLMQST
GAAFPLLEAQ ARLVAARLAG RYAPPAPAAQ RAACRAELRA ATARWGDRRP AMRVDFDTYL
AQLGRELAAG TRRAARDAT
//