ID   A0A0S7DQP8_9EURO        Unreviewed;       647 AA.
AC   A0A0S7DQP8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM36668.1};
GN   ORFNames=ALT_004556 {ECO:0000313|EMBL:GIM36668.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM36668.1};
RN   [1] {ECO:0000313|EMBL:GIM36668.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM36668.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:GIM36668.1}.
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DR   EMBL; BCLY01000004; GIM36668.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DQP8; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_2437; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF100; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G00630)-RELATED; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
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|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING         297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   647 AA;  69832 MW;  73C72BFAE4D4AF9B CRC64;
     MIIPRLFGLL AATAGVAKAV NITGYEYVVV GSGAGGGPLA ARLALAGHKT LLLEAGDDQG
     ETFNYTIPAY SARASEDEKL AWNFFVHHYA DDERQARDFK TTYETPSGEL YTGLNPPEGS
     TLMGTLYPRT GTLGGCTAHN ALIAVYPHHS DFEYISTLTG DSSWSPDNMR KYFAKLERNH
     YLLPGMEGHG YDGWLQTETA PLSIVLEDPQ LLSMLTGGAF ALGNLTDNVI NIATLLAGDA
     NADTTTRDTV SGYYQIPIST DDAHRNGARE FIIAVRDAKN TDGTKKYPLD VRMNTHVTKV
     TFDETVDPPR ATGVEFLDGQ HLYKASPLSK TASAGIPGSA TASREVIVAG GVYNSPQILK
     LSGIGPADEL NKFGIKVIKD LPGVGTNLQD HYEISVQGKI EEDFSCLNGC TFSIHDEADP
     CINRWETPIL GDRGIYSSPG LAATMLYKSS VTADDSFDIF CFGGPVNFRG YFPDYSINAT
     DEHNWFTWAI LKAHPRNTAG TVALQSANPL DVPKITFNYF DTGVGDYDAD LTALYEAIEL
     ARDAFKRQLV NVTEVLPGAA VTSKEDIENY VKDAAWGHHA SCTCPIGADD DPMAVLDSKF
     RVRGVSGLRV VDASVYPKIP GTFTAVSTYM VAEKAADEIL SELAASS
//