ID A0A0M8YEC2_9PSEU Unreviewed; 450 AA.
AC A0A0M8YEC2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=ADK67_17555 {ECO:0000313|EMBL:KOX24834.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX24834.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX24834.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX24834.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOX24834.1}.
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DR EMBL; LGED01000192; KOX24834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8YEC2; -.
DR STRING; 1415542.ADK67_17555; -.
DR PATRIC; fig|1415542.3.peg.3806; -.
DR Proteomes; UP000037722; Unassembled WGS sequence.
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 161
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 410..411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 450 AA; 50032 MW; E5AF1655EF446CCA CRC64;
MPASFRWGVA TSAYQIEGAH DEDGRGPSIW DTYCRTPGMV HNGDNGDVAC DHYHRMPEDV
ALIGSLGVDT YRFSVAWPRV QPGGKGPVNA AGMAFYDRLV DELLAKGVDP WVTLYHWDLP
QELEDAGGWP VRDTAYRFAD YSMLVFDALS DRVRHWTTLN EPWCSAMLGY YEGRQAPGRQ
DFEAAIHAVH HLLLGHGLAT RRMREAATVP MEFGITLNMS HAAPATDSAA DHDAARRADG
LSRRIYLDPL VRGHYPADVV DDLAARGVKI PEEPGDLDVI KQPIDVLGVN YYSSSKFSGV
DEAGNTEDAD GVPVCREVRY GRPVTAMDWE IVPEGFTNLL VQIGAEYPGV PMVITENGAA
FDDKADEAGF VRDDDRTAYL ESHIAAVAKA RTEGADVRGY FAWSLMDNFE WSYGYDKRFG
LVHVDYDTQV RTLKSSALWY RDTIRRVRGS
//
