ID M7UBX0_BOTF1 Unreviewed; 406 AA.
AC M7UBX0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=BcDW1_76 {ECO:0000313|EMBL:EMR91254.1};
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:EMR91254.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; KB707674; EMR91254.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UBX0; -.
DR STRING; 1290391.M7UBX0; -.
DR HOGENOM; CLU_004624_0_1_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153}.
FT DOMAIN 62..295
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 406 AA; 44729 MW; 023950F85FFC5312 CRC64;
MTEATPLLKK KGLSFDYNGS KVRGVNLGGW FVLEPWITPS LFYGSWVDEY TLTQTLGKSA
SQNLLNAHWA TWITQNDFNE IASVGLNHVR IPIGYWALNP LPGDPYVQGQ LTYLDKAIGW
ARQAGLKVIL DVHGAPGSQN GFDNSGRKGP VTWTQGDTTK QTLAAIQTLA YRYAPATDVV
TGIELLNEPA NWALDMGAVK QFYYDGWGNV RNANPDTAVV IHDAFLSPPS WNGFMNYQSG
VNDIILDTHI YQIFSFAEVA MKPCQHVQVA CSQVGNLANT DKWTIVGEFS GAQTDCAKWL
NGFGVGSRYD GSYPGSPAWY GSCQTKDVGT VDGLLEVDKV NLAYFMEAQL DAYEAHSGWV
FWTWKTESAP EWHFQNLTRA GLIPQPLTSR KYGKQCATSA CLIPGN
//