ID Q59976_STRSQ Unreviewed; 479 AA.
AC Q59976;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 102.
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 Name=bgl3 {ECO:0000313|EMBL:CAA82733.1};
OS Streptomyces sp.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1931 {ECO:0000313|EMBL:CAA82733.1};
RN [1] {ECO:0000313|EMBL:CAA82733.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=QM-B814 {ECO:0000313|EMBL:CAA82733.1};
RX PubMed=8055926; DOI=10.1111/j.1432-1033.1994.tb19025.x;
RA Perez-Pons J., Cayetano A., Rebordosa X., Lloberas J., Querol E.;
RT "A beta-glucosidase gene (bgl3) from Streptomyces sp. strain QM-B814.
RT Molecular cloning, nucleotide sequence, purification and characterization
RT of the encoded enzyme, a new member of family 1 glycosyl hydrolases.";
RL Eur. J. Biochem. 223:557-565(1994).
RN [2] {ECO:0007829|PDB:1GNX}
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
RA Guasch A., Vallmitjana M., Perez R., Querol E., Perez-Pons J.A., Coll M.;
RT "Beta-Glucosidase from Streptomyces.";
RL Submitted (OCT-2001) to the PDB data bank.
RN [3] {ECO:0007829|PDB:1GON}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RA Guasch A., Vallmitjana M., Perez R., Querol E., Perez-Pons J.A., Coll M.;
RT "Crystal Structure of a Family 1 Beta-Glucosidase from Streptomyces.";
RL Submitted (OCT-2001) to the PDB data bank.
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; Z29625; CAA82733.1; -; Genomic_DNA.
DR PIR; S45675; S45675.
DR PDB; 1GNX; X-ray; 1.68 A; A/B=1-479.
DR PDB; 1GON; X-ray; 2.20 A; A/B=1-479.
DR PDBsum; 1GNX; -.
DR PDBsum; 1GON; -.
DR AlphaFoldDB; Q59976; -.
DR SMR; Q59976; -.
DR DrugBank; DB02772; Sucrose.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR BRENDA; 3.2.1.206; 1284.
DR EvolutionaryTrace; Q59976; -.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1GNX, ECO:0007829|PDB:1GON};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:CAA82733.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:CAA82733.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001}.
FT REGION 317..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 383
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 437..438
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 479 AA; 52383 MW; 9962702D8AB7436F CRC64;
MVPAAQQTAT APDAALTFPE GFLWGSATAS YQIEGAAAED GRTPSIWDTY ARTPGRVRNG
DTGDVATDHY HRWREDVALM AELGLGAYRF SLAWPRIQPT GRGPALQKGL DFYRRLADEL
LAKGIQPVAT LYHWDLPQEL ENPGGWPERP TAERFAEYAA IAADALGDRV KTWTTLNEPW
CSAFLGYGSG VHAPGRTDPV AALRAAHHLN LGHGLAVQAL RDRLPADAQC SVTLNIHHVR
PLTDSEADAD AVRRIDALAN RVFTGPMLQG AYPEDLVKDT AGLTDWSFVR DGDLRLAHQK
LDFLGVNYYS PTLVSEADGS GTHNSDGHGR SAHSPWPGAD RVAFHQPPGE TTAMGWAVDP
SGLYELLRRL SSDFPALPLV ITENGAAFHD YADPEGNVND PERIAYVRDH LAAVHRAIKD
GSDVRGYFLW SLLDNFEWAH GYSKRFGAVY VDYPTGTRIP KASARWYAEV ARTGVLPTA
//
