ID A0A2H3JFP8_WOLCO Unreviewed; 553 AA.
AC A0A2H3JFP8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dimethylaniline monooxygenase {ECO:0000313|EMBL:PCH40375.1};
GN ORFNames=WOLCODRAFT_162310 {ECO:0000313|EMBL:PCH40375.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH40375.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH40375.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH40375.1,
RC ECO:0000313|Proteomes:UP000218811};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KB468053; PCH40375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3JFP8; -.
DR STRING; 742152.A0A2H3JFP8; -.
DR OMA; DPYYVGH; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000218811; 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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
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 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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:PCH40375.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..553
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013749528"
SQ SEQUENCE 553 AA; 62171 MW; 5FDC666997070038 CRC64;
MVNVLQLVLS LLPLSGFWDR PQSTLNVLHD AFVHDSVEPP PTEPTKSIAI VGAGSAGLGV
LKAILDLPES IREDWEVVLY EQRRAVGGVW LPDPPGYHVE PPEVPETPLY PRLHTNTPHP
TMTYPHFPFP PGTPLYPDWE AVLNYHVDFA AHYNLTPHIN LNHTVVFAKW HAHDGTGDWH
VEVHAQHGED EDEVVIRRTF DHLIVANGHN HYPHYPTWDG TKGWLANSQQ GKPARQILHS
VYYREPEKFA NLSVIVVGSG ASGRDMAQQI EPLARVVYQS IRETKETAPD TTVTPKPPIA
YLTNYSVIFE DGTELFDIDA ILLGTGYEFR IPFLSSPQSS VLLTDPATSF NSSTAQTLTT
NLRYIFPLYQ HIFSLAPTVP PTALTFIGLP VLIANCPSDF AQGQIVAHAL ANASLLPSHD
EMLNDLISRE RSVSARGYDP YYEGHRLVDG DTEAQDYQDS LVDYLKKNGA IPDDGRKYVE
PWRRASRSQA PLLLRAWKRA GKLGEQERWL AGIETEDEWA DLMARLAEWQ REWENTHPAL
VASTYSSPEW LYE
//
