ID   BGLB_THEBI              Reviewed;         473 AA.
AC   P38645;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Thermostable beta-glucosidase B;
DE            EC=3.2.1.21;
DE   AltName: Full=Amygdalase;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
GN   Name=bglB;
OS   Thermobispora bispora (Microbispora bispora).
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Thermobispora.
OX   NCBI_TaxID=2006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 15568;
RX   PubMed=1482172; DOI=10.1128/aem.58.11.3455-3465.1992;
RA   Wright R.M., Yablonsky M.D., Shalita Z.P., Goyal A.K., Eveleigh D.E.;
RT   "Cloning, characterization, and nucleotide sequence of a gene encoding
RT   Microbispora bispora BglB, a thermostable beta-glucosidase expressed in
RT   Escherichia coli.";
RL   Appl. Environ. Microbiol. 58:3455-3465(1992).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable, retains about 70% of its activity at 60 degrees
CC         Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Shows greater activity against cellobiose than against
CC       aryl-beta-D-glucosides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M97265; AAA25311.1; -; Genomic_DNA.
DR   PIR; A48949; A48949.
DR   AlphaFoldDB; P38645; -.
DR   SMR; P38645; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-KW.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR03356; BGL; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Cytoplasm; Glycosidase;
KW   Hydrolase; Polysaccharide degradation.
FT   CHAIN           1..473
FT                   /note="Thermostable beta-glucosidase B"
FT                   /id="PRO_0000063878"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        378
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   473 AA;  52228 MW;  8F2188F1C93007CA CRC64;
     MTESAMTSRA GRGRGADLVA AVVQGHAAAS DAAGDLSFPD GFIWGAATAA YQIEGAWRED
     GRGLWDVFSH TPGKVASGHT GDIACDHYHR YADDVRLMAG LGDRVYRFSV AWPRIVPDGS
     GPVNPAGLDF YDRLVDELLG HGITPYPTLY HWDLPQTLED RGGWAARDTA YRFAEYALAV
     HRRLGDRVRC WITLNEPWVA AFLATHRGAP GAADVPRFRA VHHLLLGHGL GLRLRSAGAG
     QLGLTLSLSP VIEARPGVRG GGRRVDALAN RQFLDPALRG RYPEEVLKIM AGHARLGHPG
     RDLETIHQPV DLLGVNYYSH VRLAAEGEPA NRLPGSEGIR FERPTAVTAW PGDRPDGLRT
     LLLRLSRDYP GVGLIITENG AAFDDRADGD RVHDPERIRY LTATLRAVHD AIMAGADLRG
     YFVWSVLDNF EWAYGYHKRG IVYVDYTTMR RIPRESALWY RDVVRRNGLR NGE