ID Q9RA58_9DEIN Unreviewed; 423 AA.
AC Q9RA58;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 79.
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};
OS Thermus sp. Z-1.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=108325 {ECO:0000313|EMBL:BAA86923.1};
RN [1] {ECO:0000313|EMBL:BAA86923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z-1 {ECO:0000313|EMBL:BAA86923.1};
RA Takase M., Horikoshi K.;
RT "Purification and properties of a beta-glucosidase.";
RL Agric. Biol. Chem. 51:559-560(1989).
RN [2] {ECO:0000313|EMBL:BAA86923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z-1 {ECO:0000313|EMBL:BAA86923.1};
RA Takase M.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB034947; BAA86923.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RA58; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
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 164
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 392..393
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 423 AA; 47742 MW; 5873F977BFEB8AFD CRC64;
MTENAEKFLW GVATSAYQIE GATQEDGRGP SIWDAFAQRP GAIRDGSTGE PACDHYRRYE
EDIALMQSLG VGAYRFSVAW PRILPEGRGR INPKGLAFYD RLVDRLLASG ITPFLTLYHW
DLPLAQEERG GWRSRETAFA FAEYAEAVAR ALADRLPFFA TLNEPWCSAF LGHWTGEHAP
GLRNLEAALR AAHHLLLGHG LAVEALRAAG AKRVGIVLNF APRYGEDPEA VDVADRYHNR
FFLDPILGKG YPESPFRDPP PVPILSRDLE LVARPLDFLG VNYYAPVRVA PGTGTLPVRY
LPPEGPATAM GWEVYPEGLY HLLKRLGREV PWPLYVTENG AAYPDLWTGE AVVEDPERVA
YLEAHVEGRL RAREEGVDLR GYFVWSLMDN FEWAFGYTRR FGLYYVDFPS QRRIPKRSAL
WYQ
//
