ID   A0A137QPU2_9AGAR        Unreviewed;       506 AA.
AC   A0A137QPU2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Reticuline oxidase {ECO:0000313|EMBL:KXN89297.1};
GN   ORFNames=AN958_05801 {ECO:0000313|EMBL:KXN89297.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN89297.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN89297.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN89297.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) 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 oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; KQ962094; KXN89297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QPU2; -.
DR   STRING; 1714833.A0A137QPU2; -.
DR   OrthoDB; 1094055at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
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; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..506
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007295527"
FT   DOMAIN          60..233
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   506 AA;  55162 MW;  B5F5AC66370D9F4C CRC64;
     MRMIMRRFSL LATYYFLLGS LFTLSLALSL VDELRNDGIE LVAPGDSSFG SASAAFNHRF
     TFHPTAVTFP QTPEQVSTIV QTAVKYNTHV SARSGGHSYI ANGLGGRNGT LVIDLNRHLT
     GIQVDNAAGT ATIQSGNRLG DIALALNEQG RGIGHGTCPY VGIGGHASFA GFGYASRLWG
     MAIDAIVEIN LVLANGTTVT ASKSRNSELF WGMRGAGPSF GITTSITVQT FPVPPSATVF
     TYNWDMAADK ASSAVQAYQS FSLGQVPPEF GSEFMLYKGS KKGRVGMTLQ GVWFGDADLF
     EDTINPLLNQ IDQQPQETHV QPGSYINSVA FFGDEDGRLN TTGIPDGNDN FYVKSLLTPE
     SQPIATESWD AFANYLANQG FSTSLDWFIE IEEFGGPKSA VNAVPVDDTS FVTRDALFLI
     QFYGYTDDVN ANFPGSGFTL VDGMVNSIIT NMPSTWPYNA YTNYLDNRLQ DWQRLYFGQH
     YGRLQQLKAS VDPKNMFQFP TSIELP
//