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Database: UniProt
Entry: A0A067N4A8_PLEOS
LinkDB: A0A067N4A8_PLEOS
Original site: A0A067N4A8_PLEOS 
ID   A0A067N4A8_PLEOS        Unreviewed;       437 AA.
AC   A0A067N4A8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
DE   Flags: Fragment;
GN   ORFNames=PLEOSDRAFT_1050021 {ECO:0000313|EMBL:KDQ22699.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ22699.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KL198014; KDQ22699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067N4A8; -.
DR   STRING; 1137138.A0A067N4A8; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_1050021; -.
DR   HOGENOM; CLU_009665_6_3_1; -.
DR   InParanoid; A0A067N4A8; -.
DR   OrthoDB; 1947085at2759; -.
DR   Proteomes; UP000027073; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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   PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR   PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027073}.
FT   DOMAIN          295..366
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KDQ22699.1"
SQ   SEQUENCE   437 AA;  48574 MW;  30097D6AC7BA1B75 CRC64;
     GGGIGGLTFA LALGDCKSLQ VDLYEAAPRL AEKGAGITLW ERGWQIMKRL GVQADMDGLL
     QSPRNDTEAL TFEFRKGDQE PGESFYQLFL KGGPINYHRA ELQSVLLKHI SPACRFHLSR
     RLSSYSERED GVHLKFEDGT TATCDILVAA DGIKSVARGN MMEDQAKAAD AQGDDASPYL
     QCIQPFFSGS VAYRGLVRSS ILREWMPDHR TLTTPTQYWG KNKHLIVYPI SQGRFVNVVA
     FCSDPKTEGT VYDKPWTRVA EKDELLKQYE TWETEVKVLL KCLDDPTMWA IHALKPLRSY
     VSSRVVLIGD AAHAMTPHQG AGASQAIEDA YILAALVNNP RCTIASVPDV LRIYDSIRQP
     FGNRVQAASR HQGQCYELNG PGFAHILPGD KSVTSEALRI LLQDLIKGWN WQWSCSAETD
     KEQALSKLCE IDLRRAG
//
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