ID   A0A166X5J5_9PEZI        Unreviewed;       579 AA.
AC   A0A166X5J5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KZL76283.1};
GN   ORFNames=CT0861_06434 {ECO:0000313|EMBL:KZL76283.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL76283.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL76283.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL76283.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL76283.1}.
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DR   EMBL; LFIV01000016; KZL76283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166X5J5; -.
DR   STRING; 708197.A0A166X5J5; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000076552; 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:UP000076552}.
FT   DOMAIN          256..270
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         217
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   579 AA;  61047 MW;  D5319495E02D7CEB CRC64;
     MAATYDFVIV GGGVAGLVVA ARLSEVPDLQ VLVLEAGEDQ TADPRVNIPA LGPSLVKTPS
     DWQFQTVPQE GLGGREIVVP QGRLLGGSGA LNGLSFTVTT KSNVEAWTSL GNPGWDWPTF
     KEASKKTYSI TSGEGKGPLK LALPDNAESF WPKVWQDTIR GLGFADSCDP LSGQGVGSSI
     TPDTVDPETK QRSYAASTYL QSAKSRSNLT VVTGALVKKI VFKTDAGEIV AEAVQYTKDG
     ETKTVTARKE VVLTAGALNS PRLLELSGVG NAELLRGLGI DVVLDNPHVG ENLQNHVMVG
     ASFEALPEHD TMDGIVRQDP AAVGAAMEAY GKGTGPFARS GTSATAQLPL PAGEDMSQLL
     DKLSGPKTSA TPAFTKALET YVRSVVTSSS EPSGYYLSFP GYALFSGDGT MAPPPPGDEK
     YFTIAVLLAH PLSRGSSHIT SASLESHEVA IDPAYLSHPF DVEVLARHIQ LLEKIAASEP
     LRSQLKAGGK RNPTNALTDL EQAKEFVRQT AIGAHHFTGT CSMMPRELGG VVDEKLRVHG
     IRGLRVADAS IVPITVRANP QATVYAIGER AGDLIKSSL
//