ID S3C299_OPHP1 Unreviewed; 489 AA.
AC S3C299;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dimethylaniline monooxygenase {ECO:0000313|EMBL:EPE06887.1};
GN ORFNames=F503_03314 {ECO:0000313|EMBL:EPE06887.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE06887.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE06887.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE06887.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KE148152; EPE06887.1; -; Genomic_DNA.
DR AlphaFoldDB; S3C299; -.
DR STRING; 1262450.S3C299; -.
DR VEuPathDB; FungiDB:F503_03314; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_3_1; -.
DR OMA; PSYPFWN; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000016923; 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; 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; 2.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PIRSF; PIRSF000332; FMO; 3.
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:EPE06887.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923}.
SQ SEQUENCE 489 AA; 55457 MW; 1F99C31F9327D0E6 CRC64;
MAPVKSIAII GAGASGAAAA NAFAAEKYFD VIKVFERREE PGGTWIFDAV PPELDLVPGA
LPYQLDPPLR IPPALPTTVR ANTQERFHKT PVYDGLTTNV PEIAMSLSDR RFPYGPFVPH
WVPKNYIREH FSVHGHDKLL NLNTTVERVT KIAGDRWHLV LRRHDALLDR DEWWEEDFDA
VVFGNGHYSV PYVPFVPGLA EYLLKFPGRV SHSKSYRGPK QFTNQRVLVI GNSTSGYDVT
DQLRRSPLVQ HPIIQSRHSR SLWEGDEPPD GLTWKPVISE YTADGTILFE DGSSLAHSEI
DAIVYCTGYR PSYPFWDAKK NGRDLYDYEA NRFAGTFQHT FVPDYPTLGV IGIPRSLTFR
SFEYQAIALA RVWSGRAKLP SLEEQRQWEV DRVKERNLSH RKFHDVEWDT GETEEYLTFL
YRLAGLPLLD GTGLTPPVLD ASTRWAIENI RKHPIFRPTR SSAKGGQGEV ANEGDWVVVS
PWKDSLSFI
//