ID A0A1M6W306_9ACTN Unreviewed; 446 AA.
AC A0A1M6W306;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05421803_13926 {ECO:0000313|EMBL:SHK88028.1};
OS Nocardiopsis flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=758803 {ECO:0000313|EMBL:SHK88028.1, ECO:0000313|Proteomes:UP000184452};
RN [1] {ECO:0000313|EMBL:SHK88028.1, ECO:0000313|Proteomes:UP000184452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5723 {ECO:0000313|EMBL:SHK88028.1,
RC ECO:0000313|Proteomes:UP000184452};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQZK01000039; SHK88028.1; -; Genomic_DNA.
DR RefSeq; WP_073384261.1; NZ_FQZK01000039.1.
DR AlphaFoldDB; A0A1M6W306; -.
DR STRING; 758803.SAMN05421803_13926; -.
DR OrthoDB; 5166882at2; -.
DR Proteomes; UP000184452; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184452}.
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 348
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
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 288
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 401..402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 446 AA; 47832 MW; B78785EDA6D5F8CA CRC64;
MSSPFLWGVA SAAFQVEGAL AEDGRAPSVW DTFAARPGAV LDGHSPAVAC DHYHRWPQDV
ELLGRLGVNA YRFSLAWPRV VPQGSGAVNG AGLDFYDRLV DALLERGVTP FPTLFHWDLP
QALEDAGGWT SRDTARAFAD YAAAAADRLG DRVPRWITLN EPVVHMAYGH AFGIHAPGRT
LEVPEVLRVA HHLLLAHGLA AAELRSRGLE ALLTNNLTPV RSPEDPSGAD LAAGAAYDAL
HNRLFADPVL LGSYPDLSAF GAAEVPGVRE GDMEAIAGSA DGIGVNYYNP SLVLAPEEGA
GLPFSLGEIT GVPTTAFGWP VVPEGLTETL VGLTERYGEA LPPLYVTENG CSREDAVVGG
RVADPERTAY LESHIAAVDA ARERGADVRG YFVWTLTDNF EWAQGYHQRF GLVHVDHRTQ
VRTPKDSFAR YRDIIAARTG APESSG
//