ID   A0A178DQ81_9PLEO        Unreviewed;       601 AA.
AC   A0A178DQ81;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:OAL44963.1};
GN   ORFNames=IQ07DRAFT_591804 {ECO:0000313|EMBL:OAL44963.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL44963.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL44963.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL44963.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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}.
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DR   EMBL; KV441659; OAL44963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DQ81; -.
DR   STRING; 765867.A0A178DQ81; -.
DR   InParanoid; A0A178DQ81; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..601
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008084577"
FT   DOMAIN          283..297
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        537
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        580
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         115
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         251
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   601 AA;  64669 MW;  9655B8DC5223803D CRC64;
     MKFWALAVVV PSLLGPAGGT AFKRESVESI SSNSYDFIVV GGGTAGLAVA SRISAGLPHR
     TILVIEAGPD GRQEPGINIP GRKGSTLGGK YDWNLTTVAQ PNANNRVFSQ NRGKVLGGSS
     ALNLMTWDRT SIAELDAWEK LGNKGWNWKN LYAAMLKVET FLPSPAYGTE GVGKTGPIQT
     LINRIFPLHQ STWIPTFNGL GLPTNKQSLN GKPIGVSTQP SNVSPKYTRS YAPEYLKLAK
     KNLVLKLDTR VAKVNFKGKT ATGVTLEDGT VLTARREVIL SAGSFQTPGL LELSGIGNAD
     LLKSLNITVV KNLPAVGENL QDHIRIQSSY QLKPQYPSFD ALRNTTRAAI ELALYNAGQV
     SLYDYTASGY AYFPWTTVNT TTATQLRTLV ESDTSLTSAV DKIKKSYFSP ALSATVPQLE
     VIFSDGYTGL KGYPAPTSPL FGIGTFALIG VVQHPLSKGN VHIAARNISA KPTINPNYLS
     HPYDLAAATH LAKFLRTIAS SSPMRDIWET EYEPGSAVAT DEQWGAWARA NTLSIYHPIG
     TAALLPEKDG GVVDPSLRVY GVNGLRVVDA SVIPLLPSAH IQTLVYGIAE RAAEMVVRDN
     W
//