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Database: UniProt
Entry: A0A135U4W3_9PEZI
LinkDB: A0A135U4W3_9PEZI
Original site: A0A135U4W3_9PEZI 
ID   A0A135U4W3_9PEZI        Unreviewed;       610 AA.
AC   A0A135U4W3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KXH55431.1};
GN   ORFNames=CSAL01_05068 {ECO:0000313|EMBL:KXH55431.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH55431.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH55431.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH55431.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH55431.1}.
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DR   EMBL; JFFI01001726; KXH55431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135U4W3; -.
DR   STRING; 1209931.A0A135U4W3; -.
DR   OrthoDB; 3215324at2759; -.
DR   Proteomes; UP000070121; 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   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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:UP000070121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..610
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007804596"
FT   DOMAIN          304..318
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         261
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         543..544
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   610 AA;  66039 MW;  B1B5453C59DB8E77 CRC64;
     MQLTLTLLSL LAGVPAAPIK NLDRATIQDE YDFIIAGGGT AGLVLANRLS ESGKQRVLVL
     EAGPNPEVVS AYKAPGGNQF LGGTAIDWSF YTTPQEHLDG RILRYHRGRC LGGSSVTNGF
     YYGRGSASVY DDWVKVGNPG WGWDDVYPLF VKGTHFNPPT DHQVRGFDVS YKTHDPSAYA
     DGPLQLGFQG YVPPSGVGFI EAASEALQIP IVEDHNIGNS TGVKQGTGHL DAGFLRSSSY
     DSYLKQAKDR KNLDVLHFAP VWKINFDQGT EGKKPKAVGV AFMDHPTGIV HEVRAKKEVI
     ISAGAFNSPQ LLMVSGVGPT SQLNEFGIEP VHINENIGQH LNDHSVFSIM ALSTPEFSTT
     DMAATYQSLR AAQDEFYTNA TGEYTAPSGI TNAFQKLSAD ELQAIGAGDV VSAGLANQSH
     IEYLFESVFY PSGPTPYYTP RANETYISLT ASSMVALSRG NVTLRSNSMA ETPRVNPNYY
     AHPADRKIAL ASFKYLRKIL AHPRMSEYTV GPSHGEVSPG AGVSEDDEDA VLAYVRANTI
     PNWHASGTNQ MLPEDQGGVV DPRLRVYGVD GLRVVDCSVI PILPDVNIVG SVYMIGEKGA
     EMIREDWEDL
//
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