ID G1X2I1_ARTOA Unreviewed; 475 AA.
AC G1X2I1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AOL_s00007g490 {ECO:0000313|EMBL:EGX52707.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX52707.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX52707.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX52707.1}.
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DR EMBL; ADOT01000017; EGX52707.1; -; Genomic_DNA.
DR RefSeq; XP_011118693.1; XM_011120391.1.
DR AlphaFoldDB; G1X2I1; -.
DR STRING; 756982.G1X2I1; -.
DR GeneID; 22889623; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_0_1; -.
DR InParanoid; G1X2I1; -.
DR OMA; FMEWEHH; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000008784; 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; 3.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
SQ SEQUENCE 475 AA; 54059 MW; 6BE04AAA7B7D4E4F CRC64;
MVLFRMLPKI RRVAILGGGP SGVVAAKCLL SEGLTPAIFE QRSSFGGVWN YTPETKSRLE
HIPQEDPNLD DEPVPDSHGS EKPVFMSPVY NELETNIPKD LMVFNKTPFD ERLQLFPGHE
DTKLYVQEFS KGLENYTEFN RRVVKLVRKD GLQWEIETQD VVSAETEKKV FDAVIIATGH
YNVPYIPPID GIEEFERRYP GSILHSKYFR VADGYKGKRV IVVGNSASGI DIASQISEVS
QIPLYQSCRS KGAYKDFPLL APEKIKIVPT IERFVPDDRT VVFSDGTVEK NIDVILFCTG
YLHSLPFLEE SAKPSERMIT DGFYIHRLYQ HLFYIPQPTL SIVGLPTKVI PFPFVETQAA
VVAGVYSGRL GLPSEESMSK WEKDLLEQKP GDRHFHFLTF PQDADYMDIL NEWSEEKESD
GKRALYQPTK WGGKERWIRK NTPKIKAAFL VAKSEGRIVK TLEELGFHYE GDKEI
//
