ID   A0A319EMW2_ASPSB        Unreviewed;       625 AA.
AC   A0A319EMW2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:PYI08088.1};
GN   ORFNames=BO78DRAFT_365554 {ECO:0000313|EMBL:PYI08088.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI08088.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI08088.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI08088.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KZ826337; PYI08088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319EMW2; -.
DR   STRING; 1448318.A0A319EMW2; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
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:SF138; DEHYDROGENASE PKFF-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.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..625
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016234474"
FT   DOMAIN          320..334
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         79..80
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   625 AA;  69320 MW;  F2C25EE037F9B5A5 CRC64;
     MRARLLPLLF ASSLWLTPAP CSPFVYHRRP QFQQYLGPDA QENPSQPTEP YDYVVVGGGV
     TGLIAAARLA EFYNVAVIER GGYYETVAGD KSEIPAYDEN WDNPPQDSLE YWWEVPPSPE
     TNGRTLNFTS GKMVGGSHDF SYFGYLRPSV GSLQKWADEV DDQSWTYQNT EKYFDKSVFF
     TPPNSTSRWA NATPEYDPSS LQGTGPLEIS YPRWAHPFGT WIRKSLDAMG VSHALSFATG
     ELFGSSWVLD LINSTDGKRA TTWTAFVKDK PHKKKLDLFT DTLAEKILFD GKTATGVAVT
     RNLTEHFTIK AKNEVVLAGG AILSPQLLMV SGVGPADELK KWDITPVLDS PSVGQHMQDH
     IVVTVTYKVD VPTTSILLHE EAKKKNIQLF RNNLSGMLFN PGPDFGLGYD IPKDMRNFSR
     EAREDLGSFP KDWPEVVMVS FPMGKSWPDD GNYASLASIP MTVVSRGNVT ITSSQMTDKA
     LVRPGWLTSH TDLEVAVGAV KYMRAVFENP AMAEILASDE ISPGTEAVTW TELEDAVRSG
     YRSMHHAGCT LRMGRKNDPN AVVDPTGKVI GLDNVRVVDV SVFPFLPPAL PLATAFMVSE
     KITDHIITEQ QSKDRHGHDK LRLDL
//