ID   Q9RA61_THETH            Unreviewed;       431 AA.
AC   Q9RA61; Q9X9D4;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=bglT {ECO:0000313|EMBL:AAD32630.2};
GN   Synonyms=b-gly {ECO:0000313|EMBL:CAB42553.3};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274 {ECO:0000313|EMBL:AAD32630.2};
RN   [1] {ECO:0000313|EMBL:CAB42553.3}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HB27 {ECO:0000313|EMBL:CAB42553.3};
RX   PubMed=10580648; DOI=10.1023/A:1006997602727;
RA   Dion M.P., Fourage L., Colas B., Hallet J.H.;
RT   "Cloning and expression of a beta-glycosidase gene from Thermus
RT   thermophilus. Sequence and biochemical characterization of the encoded
RT   enzyme.";
RL   Glycoconj. J. 16:27-37(1999).
RN   [2] {ECO:0000313|EMBL:AAD32630.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TH125 {ECO:0000313|EMBL:AAD32630.2};
RX   PubMed=10741834; DOI=10.1007/s007920050134;
RA   Fridjonsson O., Watzlawick H., Mattes R.;
RT   "The structure of the alpha-galactosidase gene loci in Thermus brockianus
RT   ITI360 and Thermus thermophilus TH125.";
RL   Extremophiles 4:23-33(2000).
RN   [3] {ECO:0000313|EMBL:CAB42553.3}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HB27 {ECO:0000313|EMBL:CAB42553.3};
RA   Dion M.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0007829|PDB:3ZJK}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RX   PubMed=24287187; DOI=10.1093/PROTEIN/GZT057;
RA   Teze D., Hendrickx J., Czjzek M., Ropartz D., Sanejouand Y.H., Tran V.,
RA   Tellier C., Dion M.;
RT   "Semi-rational approach for converting a GH1 beta-glycosidase into a beta-
RT   transglycosidase.";
RL   Protein Eng. Des. Sel. 27:13-19(2014).
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; AF135400; AAD32630.2; -; Genomic_DNA.
DR   EMBL; Y16753; CAB42553.3; -; Genomic_DNA.
DR   RefSeq; WP_011174517.1; NZ_CP053288.1.
DR   PDB; 3ZJK; X-ray; 2.20 A; A/B/C=1-431.
DR   PDBsum; 3ZJK; -.
DR   AlphaFoldDB; Q9RA61; -.
DR   SMR; Q9RA61; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   BRENDA; 3.2.1.21; 2305.
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:3ZJK};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:AAD32630.2};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:CAB42553.3};
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   431 AA;  48612 MW;  D6F7993D61D985E5 CRC64;
     MTENAEKFLW GVATSAYQIE GATQEDGRGP SIWDAFAQRP GAIRDGSTGE PACDHYRRYE
     EDIALMQSLG VRAYRFSVAW PRILPEGRGR INPKGLAFYD RLVDRLLASG ITPFLTLYHW
     DLPLALEERG GWRSRETAFA FAEYAEAVAR ALADRVPFFA TLNEPWCSAF LGHWTGEHAP
     GLRNLEAALR AAHHLLLGHG LAVEALRAAG ARRVGIVLNF APAYGEDPEA VDVADRYHNR
     FFLDPILGKG YPESPFRDPP PVPILSRDLE LVARPLDFLG VNYYAPVRVA PGTGTLPVRY
     LPPEGPATAM GWEVYPEGLH HLLKRLGREV PWPLYVTENG AAYPDLWTGE AVVEDPERVA
     YLEAHVEAAL RAREEGVDLR GYFVWSLMDN FEWAFGYTRR FGLYYVDFPS QRRIPKRSAL
     WYRERIARAQ T
//