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Database: UniProt
Entry: A0A066WVC5_COLSU
LinkDB: A0A066WVC5_COLSU
Original site: A0A066WVC5_COLSU 
ID   A0A066WVC5_COLSU        Unreviewed;       617 AA.
AC   A0A066WVC5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative GMC oxidoreductase {ECO:0000313|EMBL:KDN60843.1};
GN   ORFNames=CSUB01_04644 {ECO:0000313|EMBL:KDN60843.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN60843.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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}.
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:KDN60843.1}.
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DR   EMBL; JMSE01001467; KDN60843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066WVC5; -.
DR   STRING; 1173701.A0A066WVC5; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_5_1_1; -.
DR   OMA; IMRRTKM; -.
DR   OrthoDB; 2392848at2759; -.
DR   Proteomes; UP000027238; 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:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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:UP000027238}.
FT   DOMAIN          287..301
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         240
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         545..546
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   617 AA;  67558 MW;  2F2CEDE672A92DCB CRC64;
     MGIYSKLADD IQEVDVILAG GKYRYCGTAA CVLAGRLTAS DPNLSILVIE GGTNNRDVPS
     VVHPAFFLDH LAPDSKTAIF YQGNKSDQLA GRSPIIPAGG ILGGGSSINF MLYTRAQKAD
     FDSWRTPGWS TADLRPYLNR FETYHGNGDP SHHGHSGPVH VSSGGFRLNS AEDDILAAAK
     QTGYPEIRDL QNLDDNNGYE RWMRYVSPEG RRQDAAHTFL HPRLEDGKHP NLHVVVESKV
     VRVLFDDKKR AVGVEYTPNP QYQAVLSTTK QPVRSVRARK MVVLSCGACG TPGVLERSGL
     GDKKILDRAG VPVVADLPGV GHDYQDHHLA LYPYKTALKP DETLDDILSG RISHEEAVEK
     KHKMLGWNGV DVVSKIRPSE EEVKALGPEF EKAWERDFKN DPNRPVMLSG FLHGYLGDHA
     AIPQGQYTTA ANYTAYPYSR GSIHITGPSL SDPLDFDTGF FSDPDDIDLK KQVWAYKHSR
     EVARRTALYR GELAGGHPSF PEGSKAALVD SVPADAHKTV TPLEYSEADD RAIEQFLREN
     INTTWHSLGT AKMAPREDLG VVDSSLSVYG VERLKVVDLS IVPENVAANT NNTAFVVGEK
     AADIIANELG IVISSKL
//
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