BGL1_PASFU
ID BGL1_PASFU Reviewed; 40 AA.
AC P85516;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Beta-glucosidase 1;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase;
DE AltName: Full=Cellobiase;
DE AltName: Full=Gentiobiase;
DE Flags: Fragments;
OS Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX NCBI_TaxID=5499;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RA Zhao X.S., Gao L., Wang J., Du X.L., Gao J., Zhou Y.F., Tai G.H.;
RL Submitted (MAR-2008) to UniProtKB.
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:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.18 mM for pNPG {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1};
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DR AlphaFoldDB; P85516; -.
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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation.
FT CHAIN <1..>40
FT /note="Beta-glucosidase 1"
FT /id="PRO_0000370227"
FT NON_CONS 9..10
FT /evidence="ECO:0000305"
FT NON_CONS 24..25
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 40
SQ SEQUENCE 40 AA; 4184 MW; 9B7085022AB31854 CRC64;
LVAHEENVRV GKDEGFAKAG GLSRLPLEAG ESGTATFNVR