ID A0A1A9B3M3_9ACTN Unreviewed; 455 AA.
AC A0A1A9B3M3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=GA0070622_1059 {ECO:0000313|EMBL:SBT64090.1};
OS Micromonospora sediminicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=946078 {ECO:0000313|EMBL:SBT64090.1, ECO:0000313|Proteomes:UP000199558};
RN [1] {ECO:0000313|EMBL:SBT64090.1, ECO:0000313|Proteomes:UP000199558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45794 {ECO:0000313|EMBL:SBT64090.1,
RC ECO:0000313|Proteomes:UP000199558};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|RuleBase:RU361175}.
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DR EMBL; FLRH01000003; SBT64090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A9B3M3; -.
DR STRING; 946078.GA0070622_1059; -.
DR OrthoDB; 3182512at2; -.
DR Proteomes; UP000199558; 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; 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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175}.
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 165
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 409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 416..417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 455 AA; 49515 MW; 956B32180AE9B76B CRC64;
MTGLRFPEGF VWGAATAAYQ IEGAAREDGR GPSVWDTFSR TPGAVFQGHT GDVACDHYHR
YADDVAVMAE LGLRAYRFSV AWPRVRPDGT GPVEPRGLDF YDRLTDTLLD AGIDPIVTLY
HWDLPQGLED RGGWTVRETA EHFADYAVAV HQRLGDRIRT WTTLNEPWCS AYLGYGNGVH
APGRRDAGDA FRAVHHLLLG HGLAARALRA AGAETLGITL NLADVQPADA GSAADADAVR
LVDGLHNRIF LDPLTGAGYP EDVLAHVSRI VPTDFVRDGD EKMIAAPLDL LGLNYYSPTY
VAGRADGGGS DAYPGTAGSV EFLPATGALT DMGWSIEPAG LTRLLERVAA DHPGLPLMIT
ENGGAFPDSA RDEQGRVADT DRTAYLDGHL RAAHAAIARG VDLRGYLVWS LLDNFEWAEG
YRKRFGIVHV DYLTQRRTPK QSARWYQEVI ARNGL
//
