ID   A2462_ARTBC             Reviewed;         430 AA.
AC   D4B1Y1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable FAD-dependent monooxygenase {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_02462;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000028; EFE30542.1; -; Genomic_DNA.
DR   RefSeq; XP_003011182.1; XM_003011136.1.
DR   AlphaFoldDB; D4B1Y1; -.
DR   SMR; D4B1Y1; -.
DR   STRING; 63400.XP_003011182.1; -.
DR   EnsemblFungi; EFE30542; EFE30542; ARB_02462.
DR   GeneID; 9523839; -.
DR   KEGG; abe:ARB_02462; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_3_2_1; -.
DR   OMA; EIKLADW; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Glycoprotein; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..430
FT                   /note="Probable FAD-dependent monooxygenase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434485"
FT   BINDING         9..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         307..330
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   430 AA;  47758 MW;  E103F1A3AF70872B CRC64;
     MGSTSTPPHV LIIGAGITGL ALAQALRKHG VSFAVYERDP DPLHRGKGWG LTIHWSLDAF
     LRLLPQHLID RLPETYVDPD AVAKGENGNF LLFDLRTGET KWKVPPAKRL RVSRERLRRL
     LMDGIDVQWN KTISSISQIS ETAVRCEFSD NSSAEGTLLV GCDGSRSKTR SLLCSLAGNE
     TPVRSENYQL PVRLIGVSAA LPSRIALKMR ALDPFFLQAG DPATSNFFWF SFLDTPINND
     REDRDTYECQ ILISWPYRKD GSNNIEIPCH NVDKIKLMHS LADGWVEPFC EVVQSIPEET
     EPKIISLEDW PTPPKGSWSN LGGTATLVGD SAHAMTMFRG EAGNHGILDV SNLLEALIPV
     LTSSPHSPAK TQEEVINEYE DEMTTRTRPA VLRSRKACLD AHDYPSITAD SPLVARRGAF
     EDDDLEYLLN