ID M7UKG9_BOTF1 Unreviewed; 888 AA.
AC M7UKG9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=BcDW1_7284 {ECO:0000313|EMBL:EMR84097.1};
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:EMR84097.1, 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=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448,
CC ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; KB707966; EMR84097.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UKG9; -.
DR STRING; 1290391.M7UKG9; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF27; BETA-GLUCOSIDASE; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161}.
FT DOMAIN 446..606
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 97611 MW; 525DFABC0EB74154 CRC64;
MSESPDSQIS DPIFDRFEEG SDILSSRDTI ATPNSEMTPP ESPVEKHAIL DPRTKSRQLA
ASLSLEEQVS LLVAADFWRS KSIPSKGVPA FKTSDGPNGA RGAIFKAGTK AALFPCGISL
AATWNTDLIH EVGQHLADET KARSAQVLLA PTVCLHRGPL GGRNFESFSE DPYLTGKLAI
AYIKGLQEKG IAATIKHFVA NEQETFRLTI DSVVQERPLR ELYLRPFEMA IREANPWAVM
SSYNLINGVH ADCNFHTLRE ILREEWSYDG LVMSDWGGTN SIVESIEAGC DIEMPVSTKW
RGAKAIEAVK NGELSREAVE KAAANVLYLV ERTKGSDMTP EAPEAEDDRE ETRKLIRRAG
VEGLTLLKNK DNILPIKSSQ TKVAVIGPNA NRAIAGGGGS ASLNPYYNTI PLDSIKAIPG
IDVTYALGCH TYKWLPLAAD YCTTSTGAQG VTLEFHIGDK FEGAPRIIQH RTNTDLFLWD
SVPEEVNPIW SVRAKTILTP TTTGLHTLSF SSVGPGRLLV NGDVKVDLWN WTDLGEAMFS
GSKDILFDIF LEANVPVQLV AETTNEIRPL SKQAQVNQTH ATGGCRIGYK EADAENYLQK
AIDAAKSSDV AIVIVGLDAE WESEGYDRQT MDLPSDGSQD RLIDAIVDAN PNTIVVNQSG
SPVTMPWAKK VPAILQAWYQ GQEAGNALAD VLFGFENPSG KLPTTFPVRL SDNPTYHTWP
GENLRSLYGE GLYIGYRHYD HLSLPPLFPF GHGLSYTTFS YSAPTLSSQT FSSSNQDRIT
LSLNIKNTGP RKGKEIVQLY IHDVKSSLVR PEKELKGFAK VELEAGEEKS VDIVIDKYAL
GYWDESLRNG KGLWIAEEGE FEAWVGASAE DIRQKTSFEV KESFTWIF
//
