ID   A0A0L6WGG4_9AGAR        Unreviewed;       537 AA.
AC   A0A0L6WGG4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pentachlorophenol 4-monooxygenase {ECO:0000313|EMBL:KNZ74657.1};
GN   ORFNames=J132_06611 {ECO:0000313|EMBL:KNZ74657.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ74657.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007801}.
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DR   EMBL; KQ412647; KNZ74657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WGG4; -.
DR   STRING; 1306850.A0A0L6WGG4; -.
DR   OrthoDB; 2086756at2759; -.
DR   Proteomes; UP000053712; 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.30.70.2450; -; 1.
DR   Gene3D; 3.40.30.120; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:KNZ74657.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT   DOMAIN          2..220
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          257..330
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   537 AA;  59732 MW;  EA798886A0405FC7 CRC64;
     MPRTLEIFNS FGCVDDVLKR AIPPPLTRRY ELPKGTHPIG EFDMSPHIEP TPSCPYNNIV
     LLGQSHVEGI LRDTLAKLQC QVEIGTELVS FEQNETGVNV HLLRHGSDGS NVEGVPEHGS
     FDWMIGADGA RGIVRKMSGF SFLGETRTIE NHVVGDVYVE GLSQKYWHMW GDASSMLVSF
     RPTETPGLFS FVIAGHKVNH SLLSSNEEVL RKCFAENTGS KTGLKFKEIP WVNHYMFVAP
     PRFEIHVPNP LISPNIRMVE TFQKGRVFLA GDSAHVHSFT GGQGINTGVQ DAYNLGWKLA
     LVQRGLASSS LLRTYSEERI PVIREMLDRT TRILKRTFTE KASESWNKAN GLLQLGINYR
     WSSVVLDERK RAEDAEFSDF DFGDEEEEEP CSAIDAYGGS TEGTLRAGDR APDATALVDI
     SKRAVTYRLF NIFSPGHHTV LIFSRALDRC PAIVRALKEL PPDVVRSVVL LRRGQGIPAY
     CQGVTSVFED RDGHAHDAYA ITDEWAVVVI RPDAVVGAIV GGAEGLRSYF SKIFMRR
//