ID   J5JN76_BEAB2            Unreviewed;       666 AA.
AC   J5JN76;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Glucose-methanol-choline (Gmc) oxidoreductase {ECO:0000313|EMBL:EJP66678.1};
GN   ORFNames=BBA_04618 {ECO:0000313|EMBL:EJP66678.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP66678.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP66678.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66678.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
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; JH725159; EJP66678.1; -; Genomic_DNA.
DR   RefSeq; XP_008597937.1; XM_008599715.1.
DR   AlphaFoldDB; J5JN76; -.
DR   STRING; 655819.J5JN76; -.
DR   GeneID; 19887630; -.
DR   HOGENOM; CLU_002865_4_1_1; -.
DR   InParanoid; J5JN76; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000002762; 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:SF100; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G00630)-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   Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..666
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003784588"
FT   DOMAIN          372..386
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         161..164
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         318
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   666 AA;  71604 MW;  8DC920A0991BAF98 CRC64;
     MLFKAALGLV AAAASAAAAP AISNSTISDS TISNSTISNA TELAGYEYVV IGSGAGGGPL
     AARLAMAGHK TLLIEAGDDQ GDNTNYKVPA YSAKASEDES IAWNFFVHHY ADEKRQARDY
     KTSYDTPDGG LYTGLQPPAG SKMKGTLYPR TQTLGGCTAH NALVTIYPHR SDFDSIAQLT
     GDSSWSADNM RKYFVRMEKK NYGLPFEGGH GHDGWLSTET TKISLALQDP QLLSLYTGGA
     FASGKLLPAI GDLASLLLGD ANADSKSRDT TDSYYLVPIS TKDGSRVGSR EFVVSVRDAK
     DKDGNKRYPL DVRLNCHVTK VIIDESGDKP RATGVEFLDG QYLYKASPRY GTAGKGKPGK
     VNASREVIVA GGAYNSPQIL KLSGIGPREE LESLDIPVVV DLPGVGGNLQ DHYEINVQGT
     VPKDFSALKG CTFGLNGEHD TCLDKWENPT FGDRGTLATN GLPVAMFHKS SVTENGEYDN
     FLFGGPVNFR GYFPQYSINI TQDHDVFSWA ILKAHPRNNA GTVRLRSADP LDVPDITYNY
     FDTGSGDYAK DLRSMYEAVG VARDALRRQP VKVSEVLPGE DVTSQADIEQ YAKDTAWGHH
     ASCTCPIGPD GDETAVLDSS FRVRGVDGLR VVDASVYPRI PGTFTAVSTY MVGEKAADVI
     LEQNKN
//