ID A0A179FNW9_METCM Unreviewed; 476 AA.
AC A0A179FNW9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dimethylaniline monooxygenase {ECO:0000313|EMBL:OAQ67292.1};
GN ORFNames=VFPPC_08722 {ECO:0000313|EMBL:OAQ67292.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ67292.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ67292.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ67292.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ67292.1}.
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DR EMBL; LSBJ02000004; OAQ67292.1; -; Genomic_DNA.
DR RefSeq; XP_018144379.1; XM_018287379.1.
DR AlphaFoldDB; A0A179FNW9; -.
DR GeneID; 28851373; -.
DR KEGG; pchm:VFPPC_08722; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000078397; Chromosome 4.
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; PR00419; ADXRDTASE.
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:OAQ67292.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000078397}.
SQ SEQUENCE 476 AA; 54050 MW; 956BB0BE4211907F CRC64;
MPATAIKRVA VIGAGPAGAI TVDALAKENV FDLIRVFERR ERPGGCWVGD TSPPPTISDV
KSLADRTADA PIGIPDKVPA STAKSDRPRF TESSVYPYLE TNISHLPMEF SQEPFPVEIS
ERSKALYGKA SPFRHWEVVR RYITSLYERN GYEDWVSFNT TVERVEKIGS EWKITLRKEG
KQSDYWWVEW FDAVLVASGH YSVPYIPDIE GLEQFEKARP GSVLHSKHFR GKDKFKNKRV
VVVGASVSAA DIAFDLTDTA TTPIHAINIG HSLNGYFGGE AFNHPKIEKL PSIARISPDR
TVHLINGTTI PNVDYIIFGT GYSWTLPFLP QVPVRNNRVP DLWQHIVWQH DPTLLFVGAV
HAGLTFKVFE WQAVYAARLL ANRAAKLPSL LEMRQWEEDR ISKRGDGAKF SLVFPDFEDY
FETLRGLAGE CEDGGRKLPR FRREWFREFL NGHELRRNMW RRINNEARGG VVKARI
//
