ID A0A0A2WJJ7_9GAMM Unreviewed; 455 AA.
AC A0A0A2WJJ7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=LF41_887 {ECO:0000313|EMBL:KGQ20351.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ20351.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ20351.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ20351.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-2014) 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:KGQ20351.1}.
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DR EMBL; JRKJ01000002; KGQ20351.1; -; Genomic_DNA.
DR RefSeq; WP_036165600.1; NZ_JRKJ01000002.1.
DR AlphaFoldDB; A0A0A2WJJ7; -.
DR STRING; 1300345.LF41_887; -.
DR PATRIC; fig|1300345.3.peg.211; -.
DR eggNOG; COG2723; Bacteria.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000030518; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030518}.
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 167
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 401
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 408..409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 455 AA; 51146 MW; 3BBE34F4A20E634A CRC64;
MTSNARRFPE GFLWGAATAA HQIEGSPMAD GAGPSIWTRF AHTPGMTVNG DTGDVACDHY
NRMKDDVALM AELGLKAYRF SVSWSRILPD GTGRVNQKGL DFYSRLVDEL LAKGIEPLLT
LYHWDLPAAL DDRGGWLNRD IAQWFAEYGS VLYRALDGRV KKWVTLNEPW VVTDGGYLHG
ALAPGHRSKY ETPIATHNLM RAHGAAVQAY REIGKHEIGL VVNIEPKYPN TQSPEDLAAT
KRAHAYMNEQ YLDVALLGKY PPELKNEIFG DAWPEWADED YALIKQKLDF IGINYYTRSV
TEATDSYPLK AGAVRQKLGT YTETGWEVFP QGLTDLLVWA KDRYGNIPTY ITENGAAFFD
PAVAEEGRVR DPLRMGYLKK HLTAIRNAID QGCDIRGYMV WSLLDNLEWS LGYSKRFGIV
HVNYGTQERT PKDSARWYSK AIQTHGASVD DPLPY
//
