ID M7TQE4_BOTF1 Unreviewed; 611 AA.
AC M7TQE4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative glucose-methanol-choline oxidoreductase protein {ECO:0000313|EMBL:EMR85761.1};
GN ORFNames=BcDW1_5586 {ECO:0000313|EMBL:EMR85761.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85761.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KB707886; EMR85761.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TQE4; -.
DR STRING; 1290391.M7TQE4; -.
DR HOGENOM; CLU_002865_6_2_1; -.
DR Proteomes; UP000012045; 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:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-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; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 15..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 237
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 611 AA; 65725 MW; C64D09F527AA7648 CRC64;
MSSNSYDFII VGGGTSGLVV AARLTEDPSV RVLLLEAGED HSADPRVITP GLWPALLGTD
MDWGFLSEPQ EALNGKKIPL SQGRLLGGST AINGQAWIAP SKYTVDAWAT FGNSSWTWDT
ISPYFQKSCT LTKPSPEAYS HLSLSYIDEK VQSKFTGPVQ TSFAEEVNDP LPKAWVDTWA
ELGYGVTGDP FSGVAVGGYV NAMNIDPVTK QRSHALSAYY EPIKTRENLV VKTSAFVEKI
LLDGKTSDVV AKGVSYIKDG KTETATVIQE VILAAGVFAT PKLLELSGIG SASLLESFDI
PVIIDNANVG ENLQDHLNAG FSFEVADGVK TVDALARQDQ AAIGAAMEAY MKEQKGPFAS
GGNFAGGFLP VVDFLTPEGK KELAKLLQEI KDDGKPFTKS HIEFVNDLLN TPTEGSGCFF
SYPAQGNFIP EAGSNDIMIS ANADAGNYFT ICSMLLHPLS RGSSHITSSN PETKVTIDPK
YLSNPLDLEV LARHVRYISK IVSSEPLKSF LKPNGKKNYG APEDMDDLEQ IKEYVKKAAL
SAWHPTSTCA MLPLEKGGVV NEKLVVYGTK NLRIVDASVF PLATRGNCQT TVYAVAEKGA
DLIKADYGVY A
//
