ID   A0A317WKY5_9EURO        Unreviewed;       611 AA.
AC   A0A317WKY5;
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:PWY86725.1};
DE   Flags: Fragment;
GN   ORFNames=BO70DRAFT_311433 {ECO:0000313|EMBL:PWY86725.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY86725.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY86725.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY86725.1,
RC   ECO:0000313|Proteomes:UP000247233};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         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:PWY86725.1}.
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DR   EMBL; MSFL01000007; PWY86725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WKY5; -.
DR   STRING; 1448321.A0A317WKY5; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_311433; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000247233; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT   DOMAIN          276..290
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         236
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   NON_TER         611
FT                   /evidence="ECO:0000313|EMBL:PWY86725.1"
SQ   SEQUENCE   611 AA;  65503 MW;  F5B6D054FC9877F1 CRC64;
     MSITEADIVI IGGGTAGLTL AARLSENPNL QVLVLEAGQD QTDDPRVQTP ALWPALVATD
     SDWKFMTAPQ TALHGKQIPL PQGRMLGGSS AMNGMAFIAN SKANVNAWGA LGNPGWDWDT
     ISPYYKKVFT LTLPSEEKRK ELGLEYVDES VNGNNGPIHA SFPDALVDPI ANAWVESLRG
     LGYPMSTDPF SGDARGGYTN AATIDPITKT RSYSANAYYL PAKARQNLHV ITGASVNKIL
     LDPLPNGDAS ATGVEYTKDN SIFTVTSNRE VILSAGTFNS PKLLELSGIG SRGALETLNI
     PVIIDNPNVG ENLQDHVLSG LSLEVEDFIA TKDDLMRRVP EVLSAAMESY KTRQFGPFTI
     GGNYSSALLP LPDLSSSEER ATILATTTTT TNTPLPTHTD PFAANLTSFV RSVLTTPTEP
     TGGYFTYPAQ SDFKGSGLST QTIESKFPEN YITICAFLLH PLSRGTCHIS STNPADPPVI
     DPRYLTHPTD LEMLARHTRL IDTIAASQPL ASMLKSGGKR SPGAPDDLRT APLDEVKEYV
     RCAGKSTFHP TSTCAMMPRE KGGVVDSRLR VWGVGGLRVV DASVIPIVPR GNTQSAVYAV
     AERAADLIRE D
//