BGLS_RHIRD
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 25-MAY-2022, entry version 93.
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; Proteobacteria; 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; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 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