ID B1VZ46_STRGG Unreviewed; 470 AA.
AC B1VZ46;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN OrderedLocusNames=SGR_1972 {ECO:0000313|EMBL:BAG18801.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG18801.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG18801.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR EMBL; AP009493; BAG18801.1; -; Genomic_DNA.
DR RefSeq; WP_012378895.1; NC_010572.1.
DR AlphaFoldDB; B1VZ46; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GeneID; 6212932; -.
DR KEGG; sgr:SGR_1972; -.
DR PATRIC; fig|455632.4.peg.2002; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_2_11; -.
DR Proteomes; UP000001685; Chromosome.
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 Gene3D; 3.20.20.80; Glycosidases; 1.
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 NCBIfam; TIGR03356; BGL; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001}.
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 374
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 428..429
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 470 AA; 51428 MW; AD3551BB77FF3DB1 CRC64;
MNPAPIPQRL LRPAPVRGLP ADFRWGVATS AYQIEGAVAE DGRTPSIWDT FCRVPGAVEG
GESGDAACDH YHRMPEDVEL VAGLGIDTYR FSLAWPRIQP GGRGPANAKG LDFYKRLVDE
VQGRGITPWI TLYHWDLPQE LEDAGGWPAR DTALRFAEYA ALAHEALGDR VEHWTTLNEP
WCSAMLGYAH GVHAPGRRDL GDAMRAVHHL LLGHGLAAGA LRDAAGNNPL ELGITLNLGT
ATPETDSAAD REACRRADGM GARLYLDPLV HGRYPEDVVA DLAAQHIELP VREGDPAAIA
APLDVLGVNF YRGMRFSGVT EDGSATGADG LPVTRVVERD LPRTAMDWEI TPTELTDLLV
RLQRDYALPT VITENGAAFD DTVAADGSVP DADRTAYLAD HIAAVVAARA QGADVRGYFA
WSLLDNFEWA YGYDKRFGIV RVDYDTQVRT LKDSAKWYRD TIRLTRRERA
//
