ID M7TBT6_BOTF1 Unreviewed; 603 AA.
AC M7TBT6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE SubName: Full=Putative alcohol oxidase protein {ECO:0000313|EMBL:EMR80881.1};
GN ORFNames=BcDW1_10490 {ECO:0000313|EMBL:EMR80881.1};
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:EMR80881.1, 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|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KB708094; EMR80881.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TBT6; -.
DR STRING; 1290391.M7TBT6; -.
DR HOGENOM; CLU_002865_5_1_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: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}.
FT DOMAIN 281..295
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 535..536
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 603 AA; 66087 MW; 7D79C5CD25C14E0B CRC64;
MAPIAPQTVD IIFAGGGTAA CVCAGRLAKA NPNLRILLVE GGKNNFQDPS VTTPAVYLSH
LTPESKTALF YKGQPSEHLN NRSPIVPAGG LLGGGSSINF LMYTRAQSID FDSWDTEGWT
GKDMLEMCKK LETFHPAGEG FDEEKHGYEG PVNVSNGGYS GKSVDAFMET IKGMGYREIV
DLQDGEECGG FSRWHRYVSP NGQRQDAAHT YIHPLLQSSS YPNLKILTES KVLRVLFDSS
TPPRATGIEY VPNEDRQPFV ALSKAIPHTI RAEKLVVVSA GALGTPQVLE RSGVGRREVL
ERCGVEVVNE LEGVGESYQD HQLLLYPYKT SLDDSETIDN ILSGRKDFVK ALEAKDPQLG
WNSVDVCSKL RPTTSEVEAL GTDFVSDWDR DFAPYPSKPL MLCAVVNAFL ADPTLVDPGQ
YITMGTYTAY PYSRGSIHIT SSTDVQNGYE FDAGFLSHPS DLKKQLWAYK MQREICRRLP
YYRGELELGH PKFSKGSAAR LSNGAIKGEI KDIEYSAEDD ALIEDWIRDN LNTTWHSVGT
CAMKPREKGG VVDKYLNVYG TQGLKICDLS MVPENVGANT NNTALAVGEK AAVIIGKELG
IEV
//
