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Database: UniProt
Entry: B1VW56_STRGG
LinkDB: B1VW56_STRGG
Original site: B1VW56_STRGG 
ID   B1VW56_STRGG            Unreviewed;       485 AA.
AC   B1VW56;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 81.
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_4738 {ECO:0000313|EMBL:BAG21567.1};
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:BAG21567.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG21567.1, 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|RuleBase:RU361175};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|RuleBase:RU361175}.
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DR   EMBL; AP009493; BAG21567.1; -; Genomic_DNA.
DR   RefSeq; WP_012380830.1; NC_010572.1.
DR   AlphaFoldDB; B1VW56; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GeneID; 6211999; -.
DR   KEGG; sgr:SGR_4738; -.
DR   PATRIC; fig|455632.4.peg.4845; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_11; -.
DR   OMA; SVWLKVY; -.
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:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
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; LACTASE-LIKE PROTEIN; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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:ARBA00023326}.
FT   REGION          322..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        388
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         435
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         442..443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   485 AA;  52712 MW;  17A676952041F315 CRC64;
     MTVVRPDTVP QQAPAATAPF PTGFLWGAAT AAYQVEGAAA EMGRTPSIWD TFSHTPGRTL
     GGDTGDVAAD HFHRYRDDVA LMKRLGLQAY RFSVSWSRVQ PTGRGPAVER GLDFYRSLVD
     ELLLAGIKPV ATLYHWDLPQ ELEDAGGWPE RATAERFAEY AAIMARALGD RVGMWTTLNE
     PWCSAFLGYG SGVHAPGRTE PAAALRAAHH LNLAHGRATE ALRANLPAAA QTSVTLNLHQ
     VRPLTGSEAD ADAARRIDAV GNRVFTGPML KGAYPEDLLA DTERIVNWGE LVRDGDLAAI
     AAPIDVLGVN YYTPTIVSTP ASGAGDTRND GHGSSDHSPW PGSEHVAFHL AEGRPVTAMN
     WSVKPEGLYD LLMDVSREHP ELPLMVTENG AAFDDAPDAD GRVHDPERIA YLRGHLEAVR
     RAAADGADVR GYFLWSLMDN FEWGYGYAKR FGAVYVDYET QLRTPKSSAH WYGEVIARHA
     LPPEA
//
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