ID   A0A0D0CIE6_9AGAR        Unreviewed;       569 AA.
AC   A0A0D0CIE6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=GYMLUDRAFT_171811 {ECO:0000313|EMBL:KIK58057.1};
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:KIK58057.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK58057.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK58057.1,
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 oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; KN834787; KIK58057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CIE6; -.
DR   HOGENOM; CLU_018354_4_2_1; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000053593; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593}.
FT   DOMAIN          115..291
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   569 AA;  63834 MW;  9D95EA3BB6516724 CRC64;
     MTALLDYLQG NTDVGTPTLS VKDCKLLPGD HAWPKKDVWN AFNSSVDGRL IKTIPIGAAC
     HTDGFDEEKC QFVRDHWREP ELHLPSSSSV MDFIFANKSC DPFTDKEDQC VIGAYVQYSV
     NVTRPEHVMK TIEFVKNHDI RFVVRNTGHD YMGRSTGTGA VSVWMYHSQG MEWVDEYTSK
     TYSGPAVKVQ AGVMGYQIAE EAKKRGLVVV VGECPTVGFA GGYVQGGGHS FITNLYGLAA
     DQTLSFEVIT TDGRLVTASP TENKDLYWAL SGGGGGTYGV VWSVTIRAFP DLGATAAYLS
     FNSQGLSRQD WWSILSAWQR GTPNFTDQGI FVSTAYNFEW FQMAPLFAPN HTVESVTELM
     KPILSLLESN QYNIKYHFSI EYHQKTPVSS QEMNNMISEF QFGGRLLPRS LWESEEGFEA
     FMETVKVILE AGCDFIWDVA LRPTLAIAGY PDNAVHPAWR NAERMFNPTV FLDYRASIDT
     VIKNQDRISQ VYDEPLRQLT PEGGGAYMNE ADYTEPDWKD AFYGSNYDRL LAIKDKWDPD
     QILYGSIAVG GDRWQERKDG RLCRSKSSS
//