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Database: UniProt
Entry: A0A495JL84_9ACTN
LinkDB: A0A495JL84_9ACTN
Original site: A0A495JL84_9ACTN 
ID   A0A495JL84_9ACTN        Unreviewed;       474 AA.
AC   A0A495JL84;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=BDK92_3130 {ECO:0000313|EMBL:RKR88799.1};
OS   Micromonospora pisi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR88799.1, ECO:0000313|Proteomes:UP000277671};
RN   [1] {ECO:0000313|EMBL:RKR88799.1, ECO:0000313|Proteomes:UP000277671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR88799.1,
RC   ECO:0000313|Proteomes:UP000277671};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) 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:RKR88799.1}.
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DR   EMBL; RBKT01000001; RKR88799.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495JL84; -.
DR   OrthoDB; 3182512at2; -.
DR   Proteomes; UP000277671; 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:UP000277671}.
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        376
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10055"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         435..436
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   474 AA;  52344 MW;  1C25D21D12F0CBF6 CRC64;
     MTSLETPPAV LAAPAEATVR FPEGFVWGAA TASYQIEGAV HDDGRGPSIW DTFSRTPGKV
     YAGHTGDVAC DHYHRYPQDV ALMADLGLQA YRFSIAWPRI QPDGSGPVNP RGLDFYDRLV
     DELIGRGIDP IVTLYHWDLP QTLEDRGGWT NRATAEHFAE YATAVYARLG DRVKTWTTLN
     EPWCSAYLGY GNGVHAPGRQ DPAAAFTAVH HLLLAHGLAG RALRAAGAQT LGITLNPTEA
     YPVDPTRPED QAAVRLVDGL ANRIFLDPML RGEYPADVLE HVARFTNLDH LRDGDEKIIN
     VPIDLLGINY YQPTYVTARE GATGGGGAYP GTDGIEFVAP VGPLTDMGWM IEPRGLTTLL
     VRISENYPGV PMVITENGAA FPDKFDRADP DADGRIPDAD RVDYLDGHLR AAHEAISRGV
     DLRGYLVWSL LDNFEWAEGY RKRFGIVHVD YLTQRRVLKD SARWYREVIR RNGL
//
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