ID   M3BY05_SPHMS            Unreviewed;       481 AA.
AC   M3BY05;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=FAD-linked reductase, C-terminal domain-containing protein {ECO:0000313|EMBL:EMF12941.1};
GN   ORFNames=SEPMUDRAFT_43979 {ECO:0000313|EMBL:EMF12941.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF12941.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF12941.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF12941.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(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; KB456264; EMF12941.1; -; Genomic_DNA.
DR   RefSeq; XP_016761062.1; XM_016908910.1.
DR   AlphaFoldDB; M3BY05; -.
DR   STRING; 692275.M3BY05; -.
DR   GeneID; 27906047; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_0_3_1; -.
DR   OMA; YQNWHAS; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000016931; 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:SF138; DEHYDROGENASE PKFF-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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT   DOMAIN          186..200
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        416
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        460
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         415..416
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   481 AA;  52279 MW;  1D30B82C6EC303ED CRC64;
     MIYNRGTYGS FQVWADLVGD DAWLFENVLP YYAKGITYSP ANATLRAANA SVPLPANPLA
     FNDTGPLHVS SPNFAQIFAS YVDGAFAESG ISSQQDFASG SLLGRQYAPL TISYPEEERS
     SSESSYLQAA LRSGRTNLKV YPNMLAKRII FNGTMTAMGV EVEAASYGNS QTFHLNATKE
     VILSAGAFQS PQLLMVSGIG PREQLEAHNI TVLADRPGVG ANMEDHLDFA PIWEINIENG
     VGAIADPAVN GPLIEEYRVN RTGPLTNAGV DYIGWEKLPE PYRSGLSAQA QADFAKFPAD
     WPEIEYEITA ASLSGTDPSK RFGTIIMIPV SPLSRGWVNI TSNNTRDLPV VNPNQLSHPS
     DREMAVQGFK RARSFFHTEA LQPILVGGNE YMPGPNVTSD EAILEYIEQS SYQNWHASCT
     CRMGKVEDPM AVVDTHAKVI GVTGLRVVDA SSFAVLPPGH PVSTVCKLSF LRIFSFLFTC
     C
//