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Database: UniProt
Entry: T0KLW0_COLGC
LinkDB: T0KLW0_COLGC
Original site: T0KLW0_COLGC 
ID   T0KLW0_COLGC            Unreviewed;       353 AA.
AC   T0KLW0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase C-terminal domain-containing protein {ECO:0000259|Pfam:PF05199};
GN   ORFNames=CGLO_03361 {ECO:0000313|EMBL:EQB56617.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB56617.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EQB56617.1}.
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DR   EMBL; AMYD01000695; EQB56617.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0KLW0; -.
DR   eggNOG; ENOG502RBWF; Eukaryota.
DR   HOGENOM; CLU_785287_0_0_1; -.
DR   OrthoDB; 1492754at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT   DOMAIN          284..342
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   353 AA;  39379 MW;  77C2E629D3917FAC CRC64;
     MVMTKDYFVD NSKLEEILDD GEYDYIVIGS GCTALAFIQQ ELGKDSDARI LCFERGEFWL
     PAHFENLPLP FKTSAWSPQP HLEDMEDFPK AMIDTARQPK FWEDAKELLH VTGADKIGDS
     VYSGLQREID QRLKDRWRHI TTTEYSEPAQ LAVGRGSVTL NLRFNKFSTP APLLKIYEEQ
     KSKNAASLDI LLNCTVKTLG AVDDDEDGKG HVHSIETTRR TIAWQGDNTK VILCASASPA
     ATILLNSFPE CRKTGLEYWH IDEHEPNKGS WKPAHPKQSE IRIPGIVHET STAFMGSNPS
     DGSSVGPKYN VHGVPNVYVT GGALFPTAGS WNPTLTMCGF AQDLARQLEK GRH
//
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