ID   A0A0D0BPA9_9AGAR        Unreviewed;       447 AA.
AC   A0A0D0BPA9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=GYMLUDRAFT_50564 {ECO:0000313|EMBL:KIK51414.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK51414.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK51414.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK51414.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KN834864; KIK51414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0BPA9; -.
DR   HOGENOM; CLU_009665_6_3_1; -.
DR   OrthoDB; 1947085at2759; -.
DR   Proteomes; UP000053593; 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; 2.
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:UP000053593}.
FT   DOMAIN          7..176
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          309..383
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   447 AA;  50289 MW;  7559F2B0F388CEE7 CRC64;
     MSSTSRLRVA ICGAGIGGLT FALALSRYPD IDIDIYESAR QLTEVGAGIG IFPRPWKIIK
     MLGLEADLLK VTETQVADGP VSSFRYRKSD QREGMEFFTL VTQGSLVLFH RADYQQTLLN
     HLPRRCRTHC SKRLRSYTQR QSGPIELFFE DGTTAFCDVL VGADGLKSSV RASLLSEKAR
     WAQAEGRWKE ASEILTHVDP VWCGTNAYRA LIPVEKLRAI APNHRVLSTP GVQYLGKHGY
     IIAYRISGGK LVNFVAFVSR HHLENTKFNG PWMSTVDPSA FASFFAHWEP DVQALIACTE
     KPMQWAIHTV RPMQSFISGR VALLGDAAHS MTPHQGSGAG QAIEDAYILA TVLGHSNTNR
     SNVHRALRIY DSIRCPAAYK VMEKCRINGR YFTFELDGFD LDHLPPKQQW DYLQQLGQTW
     VRNWEWAWTT SVDGTVQEAL RQLESRI
//