ID   A0A1V6QLZ8_9EURO        Unreviewed;       460 AA.
AC   A0A1V6QLZ8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Amine oxidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSOL_c060G03090 {ECO:0000313|EMBL:OQD90233.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD90233.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00043981}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD90233.1}.
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DR   EMBL; MDYO01000060; OQD90233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QLZ8; -.
DR   STRING; 60172.A0A1V6QLZ8; -.
DR   OrthoDB; 1771364at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
DR   Gene3D; 1.10.405.20; -; 1.
DR   Gene3D; 3.30.70.1990; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR42923:SF26; FMN REDUCTASE LOT6, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06600)-RELATED; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..460
FT                   /note="Amine oxidase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013048354"
SQ   SEQUENCE   460 AA;  50513 MW;  B845C0BFE5353EF6 CRC64;
     MYLSKFLPVI AYWMAVTVAA NVFDPENYAK ADVIVSDVVV VGGGSSGTYA AINLRKMGQS
     VVVVERKKRL GGHTNTYTDD STGLTVDYGV HTFLNSSITL EYFAHFNISL VNYTGSNATV
     SLADFNTGNP VFFYPSRNLT GWAVQIAQYP WLDSTWKIPQ PVASDLLLPL GDFLVKYNLS
     DAAFNLYFGS QGISNLLQQL TVNVMKMVDR AYLRGISGAM LSTANKNNSE IYVKALTELG
     SNALVSSTVT AAARPQGGRG VSLVVKTPMG SKLVQASKLL ITIPPNLGNM RPFNLNIEEL
     QIFSQWTSMG YYTLVLNNTG LPDGYQWINA NDSPATYHIP QQPGASEITS TRIPGVFYIW
     YRSPSHMTRL AVEQAAIRAI QNLQKAQNFT ITNPNIIKFK SHTPFKLSVS AQAIQDGFYS
     DLYALQGKRS TWYTGAAFIS HNGGVLWKFT QALLPWIVAA
//