ID A0A1X9Z8I5_9SPHI Unreviewed; 445 AA.
AC A0A1X9Z8I5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=CA265_16425 {ECO:0000313|EMBL:ARS41154.1};
OS Sphingobacteriaceae bacterium GW460-11-11-14-LB5.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae.
OX NCBI_TaxID=1986952 {ECO:0000313|EMBL:ARS41154.1, ECO:0000313|Proteomes:UP000194429};
RN [1] {ECO:0000313|Proteomes:UP000194429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAY-2017) 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|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; CP021237; ARS41154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9Z8I5; -.
DR KEGG; sbx:CA265_16425; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000194429; 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: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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000194429}.
FT ACT_SITE 167
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 21
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 409..410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 445 AA; 50585 MW; BE5E55BC3E82438D CRC64;
MINASDFGQN FLWGVATAAA QIEGTATQYG KGPSIWDTFT AKNGKIKKNH KLDPACDFYH
RYAEDLALVK LLGFKVFRFS IAWSRILPAG RGEINQEGIR FYHNLIDECL TQGITPYVTL
YHWDLPQALE DEGGWTSFSI NAAFNAFVSI CAIEYGDKVK NWIVLNEPFG YTSLGYMLGV
HAPGKTGLGN FFSAVLHTAL AQADGGKILR AEISKANIGT TFSCSEIIPS TQSDSDVLVA
RRVDCLMNRL FVEPTQGMGF PTANWDALEK FQIEYGTWRL HERMKFDFDF IGLQNYFPLV
VKYNAFIPVI QAWEVKAKSR KKPHTAMGWE VNADSFYNIV KQFAAYPNIK NILITENGAA
YHDKLINGKV EDPERIEYFK LYLKALLKLK KEGINVTGYM AWTLMDNFEW AEGFTARFGL
IYNDFKTQER SIKDSGYWWQ NFLKS
//
