ID A0A2H3GF64_FUSOX Unreviewed; 487 AA.
AC A0A2H3GF64;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Thiol-specific monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AU210_015186 {ECO:0000313|EMBL:PCD23669.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD23669.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD23669.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD23669.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD23669.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD23669.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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:PCD23669.1}.
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DR EMBL; MABQ02000011; PCD23669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3GF64; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000219602; Chromosome 13.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
SQ SEQUENCE 487 AA; 55394 MW; 9F027DE55062E716 CRC64;
MPHKIRRVAV VGAGPAGAIA TDALVKEGAF DTIRVFDRRS AVGGTWIHTP HLPPGIPSLE
RLVSGEADNE VTIPGNLPAV TTISEAVNSH QHRFSDTPIH ENLHSNIAPD IMSYTQEPFP
KELSQKTLAE YGPDSLFRHH SVVREWIEGI FSRGGHDKLL ELETTVERVE KENGEWVITL
RKVLKGRNYW WRETFDAVVV ASGHYNVPWF PKVEGLLEFD RRFPGAIHHS KHFREGSKYR
GKRVIVVGAS VSSIEIIHEI LDVVDGQVYA SIRDQPIPAF GWVPFEHPKI AIKPAIQRFD
PETGRVHFTD GSYLDNIDHI IYGTGYTFSF PFIPAVQKRV KNAYRRLPGV YQHTWNIEDP
TLTFVGMLGG GFTFRAYEWQ SVAIARFLAS RAKALPSIPE QLEWERQRVN EKRGGKDYYS
IAPDYEGFFE YLRNIAGEPA QGTYGRKLPA FDPQWLVIWG DMVAPRLENW RRKRNEAESK
LEPKSKL
//
