ID   BGLS_RHIRD              Reviewed;         818 AA.
AC   P27034;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Beta-glucosidase;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
GN   Name=cbg-1;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B3/73;
RX   PubMed=1537792; DOI=10.1128/jb.174.5.1478-1486.1992;
RA   Castle L.A., Smith K.D., Morris R.O.;
RT   "Cloning and sequencing of an Agrobacterium tumefaciens beta-glucosidase
RT   gene involved in modifying a vir-inducing plant signal molecule.";
RL   J. Bacteriol. 174:1478-1486(1992).
CC   -!- FUNCTION: Involved in modifying a vir-inducing plant signal molecule.
CC       Hydrolyzes coniferin but not cellobiose.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; M59852; AAA22082.1; -; Genomic_DNA.
DR   PIR; A42292; A42292.
DR   AlphaFoldDB; P27034; -.
DR   SMR; P27034; -.
DR   BindingDB; P27034; -.
DR   ChEMBL; CHEMBL4663; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:SF28; BETA-GLUCOSIDASE-RELATED; 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; SSF56988; Anthrax protective antigen; 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   Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..818
FT                   /note="Beta-glucosidase"
FT                   /id="PRO_0000210775"
FT   DOMAIN          386..538
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   818 AA;  88290 MW;  D016FC8F02FEF830 CRC64;
     MIDDILDKMT LEEQVSLLSG ADFWTTVAIE RLGVPKIKVT DGPNGARGGG SLVGGVKSAC
     FPVAIALGAT WDPELIERAG VALGGQAKSK GASVLLAPTV NIHRSGLNGR NFECYSEDPA
     LTAACAVAYI NGVQSQGVAA TIKHFVANES EIERQTMSSD VDERTLREIY LPPFEEAVKK
     AGVKAVMSSY NKLNGTYTSE NPWLLTKVLR EEWGFDGVVM SDWFGSHSTA ETINAGLDLE
     MPGPWRDRGE KLVAAVREGK VKAETVRASA RRILLLLERV GAFEKAPDLA EHALDLPEDR
     ALIRQLGAEG AVLLKNDGVL PLAKSSFDQI AVIGPNAASA RVMGGGSARI AAHYTVSPLE
     GIRAALSNAN SLRHAVGCNN NRLIDVFSGE MTVEYFKGRG FESRPVHVET VEKGEFFWFD
     LPSGDLDLAD FSARMTATFV PQETGEHIFG MTNAGLARLF VDGELVVDGY DGWTKGENFF
     GTANSEQRRA VTLGAARRYR VVVEYEAPKA SLDGINICAL RFGVEKPLGD AGIAEAVETA
     RKSDIVLLLV GREGEWDTEG LDLPDMRLPG RQEELIEAVA ETNPNVVVVL QTGGPIEMPW
     LGKVRAVLQM WYPGQELGNA LADVLFGDVE PAGRLPQTFP KALTDNSAIT DDPSIYPGQD
     GHVRYAEGIF VGYRHHDTRE IEPLFPFGFG LGYTRFTWGA PQLSGTEMGA DGLTVTVDVT
     NIGDRAGSDV VQLYVHSPNA RVERPFKELR AFAKLKLAPG ATGTAVLKIA PRDLAYFDVE
     AGRFRADAGK YELIVAASAI DIRASVSIHL PVDHVMEP
//