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
//