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Database: UniProt
Entry: E3QBX9_COLGM
LinkDB: E3QBX9_COLGM
Original site: E3QBX9_COLGM 
ID   E3QBX9_COLGM            Unreviewed;       550 AA.
AC   E3QBX9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:EFQ28214.1};
GN   ORFNames=GLRG_03358 {ECO:0000313|EMBL:EFQ28214.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(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; GG697340; EFQ28214.1; -; Genomic_DNA.
DR   RefSeq; XP_008092234.1; XM_008094043.1.
DR   AlphaFoldDB; E3QBX9; -.
DR   STRING; 645133.E3QBX9; -.
DR   EnsemblFungi; EFQ28214; EFQ28214; GLRG_03358.
DR   GeneID; 24408723; -.
DR   VEuPathDB; FungiDB:GLRG_03358; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_7_1_1; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000008782; 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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-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:UP000008782}.
FT   DOMAIN          264..278
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         93
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   550 AA;  60926 MW;  A3675D0830A65823 CRC64;
     MSTTQLPASD VDRYDYVIVG GGTAGCVVAS RLAESLPQKR VLLIEAGPSD FMDDRVLDLR
     KWLNLLGGEL DYDYGTTEQP MGNSHIRHSR AKVLGGCSSH NTLISFRPFE YDLKIWQSMG
     AKGWTFHDFM RIMDKLRNTV QPVHARHQNE LCLDWVNSCS SALDIPVLHN FNKHITQNGA
     LKQGVGFFSI SYNPDDGRRS SASVAYIHPF LRGEEKRPNL TVLTNAWVSK INVRGDTVTG
     VNLTLQDGSK RTVTARAETV LCAGAVDTPR LMLLSGIGPK QQLVDLGIPV IHDLPGVGEN
     LQDHPESIIM WELKKPVPPN QTTMDSDAGI FLRREPPNAA AKKTFFNPDG IPDGDIADVM
     MHCYQIPFTL NTARLGYDEP KDGYAFCMTP NIPRPRSRGR LYLTSADPSV KPALDFRYFT
     DEEGYDAATL VYGMRAARKV AEQAPFKDWI AREVAPGPAV QTDEELSLYA RRAAHTVYHP
     VGTTKMGDVR KDPLAVVDER LNVKGLKRVR IVDAGIFPTI PTINPMLTVL GVAEKAAEMI
     IDEAQETARL
//
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