ID   A0A3F3PTZ2_9EURO        Unreviewed;       602 AA.
AC   A0A3F3PTZ2;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:RDH30335.1};
GN   ORFNames=BDQ94DRAFT_161387 {ECO:0000313|EMBL:RDH30335.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH30335.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH30335.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH30335.1,
RC   ECO:0000313|Proteomes:UP000253729};
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 (JUL-2018) 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, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; KZ852061; RDH30335.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3PTZ2; -.
DR   STRING; 1341132.A0A3F3PTZ2; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000253729; 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; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT   DOMAIN          89..112
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          281..295
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         20..21
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         91
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         242
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   602 AA;  64955 MW;  1FB5A4C624F06BE1 CRC64;
     MSSSLHAPFE ADYVIVGGGT SGLVLASRLS ENDSTRSVIV LEAGKNLIDD PRVQTPALWT
     TLMGSEADWQ FLSTPQAALN NRVIKEPQGK VLGGSSGING QAFIAPTKAG IDAWNKLGAT
     GWTWENLSPY YKKATTLQLP DEATRNHIGV GWVDPEANGN SGPIKVSFPA VKESPMAKAW
     VEAFQGMGYG CTADPFSGVS TGGYSNLASV DYEKKQRSYA ATGYGLPAMG RQNVKILTEA
     TVQKILFSTS DNGAMAVGAE AKIEGQTVTV KARREVILTA GAVNTPKLLE LSGIGDKERL
     EQLSIPVIVE NSNVGENLQD HLMTGISFEV KSGIATGDPL LRQEPEAIQT AFQLYSEQKT
     GPMTIGGIQS SAYMPLTDYS GQPEAREAYL DSFPPVANER DQVIRDIYTQ EHEPTCQMFM
     FLAQANLHES GKSFVGQNLL PGNFLSLGIT QNLPFSRGAV HIASADPTVP PIIDPRYFSH
     PLDLDLMARN LLSVERLHNV KPIADYLVES GQRNHLEAFL TDLESAKKYL RDTATTSYHL
     SGTAAMLPQE KGGVVDENLR VYGTTNLRVC DASIFPLIPA ANPMSTVYAV AERAADIIKA
     EQ
//