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Database: UniProt
Entry: M7TVU4_BOTF1
LinkDB: M7TVU4_BOTF1
Original site: M7TVU4_BOTF1 
ID   M7TVU4_BOTF1            Unreviewed;       433 AA.
AC   M7TVU4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative fructosyl amine:oxygen oxidoreductase protein {ECO:0000313|EMBL:EMR85349.1};
GN   ORFNames=BcDW1_5993 {ECO:0000313|EMBL:EMR85349.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85349.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KB707905; EMR85349.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7TVU4; -.
DR   STRING; 1290391.M7TVU4; -.
DR   HOGENOM; CLU_007884_0_2_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   PANTHER; PTHR10961:SF24; HYPOTHETICAL FRUCTOSYL AMINE:OXYGEN OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          10..379
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   433 AA;  47810 MW;  681B308106AEB989 CRC64;
     MPTELTKSSR ILIVGGGTWA VSTALHLARR GYIDVTILDS YPIPSPIAAG NDVNKIVEEG
     SFTEGEDDIA MILLNKATEG WLNDSVFKPY YHSTGYIVAA DTPAALEHIE KRELPDSKSG
     FVRLTTAEDF RKTMPPGVLT GDFPGWKGVF KSSGAGWVHA RKALESAAKE ADRLGVKFIT
     GSPEGSVTSL LYEDGDVLGV KTADGKEHRG DRTILAAGAG ADALFDFKDQ LRPTAWTLGH
     IKMSEDETKL YKNLPVLFNI EKGFFMEPDE DNHELKICDE HPGYCNWIKG PDGKIRSIPF
     SKQQIPIDSS KRIRQFLLET MPHLADRPLS FARVCWCADT PDRAFLIDTP PGFASLTLAV
     GGSGHGFMHI TSVGGFVVDL MEGVLDPKLK NAFRWRPETA VNRNWKDLLG RFGGPNEIMD
     FQDVREWTDL PTR
//
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