ID   A0A166V4E3_9PEZI        Unreviewed;       553 AA.
AC   A0A166V4E3;
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=Choline dehydrogenase {ECO:0000313|EMBL:KZL74149.1};
GN   ORFNames=CT0861_10961 {ECO:0000313|EMBL:KZL74149.1};
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:KZL74149.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL74149.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL74149.1,
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:KZL74149.1}.
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DR   EMBL; LFIV01000035; KZL74149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166V4E3; -.
DR   STRING; 708197.A0A166V4E3; -.
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; 2.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..553
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007881005"
FT   DOMAIN          263..277
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        488
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        531
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         109
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         226
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   553 AA;  59816 MW;  DE9A3648465C5371 CRC64;
     MVIISPVVAT TLLAAAASGA PSRPCAKTYD FIIVGGGTAG LAVSTRLSQG LPNAKVLVIE
     AGPAGLGDER IEMPGRRGTN FGSAYDWNLT TVPQAGSNGR VWTQTRGHVL GGSSALNLFS
     YDRASAHEYD GWEELGNPGW NWNSMRNAMI KSENFTSADT HTGPPLFPAM NNLGIETNLK
     SLNGNVLGVL YSPNSIEPTH YNRSYSANSY LPLAGSNHFV LTESKVFKVN LDTTFDGAKR
     AAGVTLVDGT VLTARREVII SGGSLLSPAI LENSGIGKTD ILSAAGVEQL IDLPGVGENL
     QDHVRIQSSY ELKENFTGYD RLKYDTTYAA EQLRLWWEGK ISMYGYSGSG YTFMNWKQAL
     GSEDATVPQL EILFSDDYTG VKGYPSSGNA GYGKDYFTLI AAIMHPLSRG NVHVDPFNPL
     GPPLINPRYL SHEYHLQAAI QAIKKCRQVA LTEPLRSTWV SEYEPGLNVT TESQWREFAL
     KTTLSIYHPV GTCSMLPKAD GGVVDSSLKV YGTTNLRVVD ASIMPILISA HIQTAVYGIA
     ERAAEMIIEE ATR
//