ID A0A0D0BS22_9AGAR Unreviewed; 542 AA.
AC A0A0D0BS22;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GYMLUDRAFT_246433 {ECO:0000313|EMBL:KIK58071.1};
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:KIK58071.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK58071.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK58071.1,
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN834787; KIK58071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BS22; -.
DR HOGENOM; CLU_006937_8_0_1; -.
DR OrthoDB; 1612588at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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}.
SQ SEQUENCE 542 AA; 60678 MW; C766F614DFCD2DB9 CRC64;
MSKVQEFDAI VVGGGFSGVH QLIELRKLGL KVRLLEAGSG LGGFNSPRLT TFLPSKCSDS
PNPVYQLSDP DLWKDWTFSE KFAGGEEIQE YFKYVDRKRD LSRDISYNSL VVSAAWDDAA
NRWTVTTESG DVYRAEWVTL CVGISARNYV PTFKGIETFK GKIQHTYNWP KDYDLKGKKV
GIIGTGASGV QVIQECGPIA EHLTVFQRTP NLALPMRQAN LDPKAEENKK KTMRPYEFGR
MSQTLSGYLK DIEPKSALEV TPEERVLCWE DAWEKGGLLF WTSTYGDIFF NDEINDLAYD
FWKQKVRERI NNPEVAELLA PSKKPHPFGM KRPSLEQNYY EIFNQSNVKL VDVKKNPILE
ITPNGVKTSD GTEHELDVLV LATGFDMVNA SITSIDVRGQ DGIPIKEKWA DGVRTHLGLG
TAGYPNLFWV FGPQHPLAFS NAPSSIEPAS DWVAKCIKYC RDNGVQSITA TNEAQEAWNE
QVQAVGKMGL YYKADSWYIG ANIPGKKREM LQFAAGVPTY IKALNDSAQN GYSGWVLKKA
TA
//