ID   A0A178BCS4_9PLEO        Unreviewed;       580 AA.
AC   A0A178BCS4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:OAL06598.1};
GN   ORFNames=IQ06DRAFT_208603 {ECO:0000313|EMBL:OAL06598.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL06598.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL06598.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL06598.1,
RC   ECO:0000313|Proteomes:UP000077206};
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; KV441705; OAL06598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178BCS4; -.
DR   STRING; 765868.A0A178BCS4; -.
DR   InParanoid; A0A178BCS4; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000077206; 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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT   DOMAIN          270..284
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        515
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        559
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         230
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         560..561
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   580 AA;  63502 MW;  5E76036A48214075 CRC64;
     MTDVNIADGS SKSYDYVICG GGTAGCVLAR RLAEIPNTSI LVLEAGKPKN EVPASSIPAG
     VSQILGTDAD WNIQSEPCVE LNNRRLHLAR GKFVGGSSGC NGTLCIRGVP QDYDDWGVDG
     WSGADMFAYM KKAEQFRNKD WFDAVLEEHG EDGPLITAPH DPAPISSRVL ESFESKGLQL
     RPDMFTTGET SQGCGHAVRS IHQGVRTASY DYLGNEESRV GIDIVTGRYV DKIILEERAN
     EVVATEVVMQ DAEGQTHHVR ARKEIILTSG AYGSPAILLR SGIGPASELT DYGIATHINL
     SGVGKNLQDH LVVLNFYEVL EPGLTNDHLI LHTGAKERTA QEYKTSCTGF LSQFPFGVFA
     YARLDERLKD NSLWQESRLS ADRDAMGTLL SQPHVEFWNT ECYSPKYMFK DFPPDGKYAF
     AMATTFFSAK SRGELKLAST DPTANPKVQH NYLVDPLDML VFSEACRLAN EIAIEGAGTK
     DVVVGSWPTA QRHDTYTARE QWQEAIRERA DTCYHPGGTC KMGNADDEMA VVDAELRVRG
     VTNLRVVDAS VMPLLPSGHP QMTVFAIAEK AADIIKAGRR
//