ID A0A2W2DK39_9ACTN Unreviewed; 465 AA.
AC A0A2W2DK39;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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=C1I93_03465 {ECO:0000313|EMBL:PZG00118.1}, Jiend_48970
GN {ECO:0000313|EMBL:BCJ61475.1};
OS Micromonospora endophytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=515350 {ECO:0000313|EMBL:PZG00118.1, ECO:0000313|Proteomes:UP000248627};
RN [1] {ECO:0000313|EMBL:PZG00118.1, ECO:0000313|Proteomes:UP000248627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45430 {ECO:0000313|EMBL:PZG00118.1,
RC ECO:0000313|Proteomes:UP000248627};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella endophytica.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BCJ61475.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 109090 {ECO:0000313|EMBL:BCJ61475.1};
RA Komaki H., Tamura T.;
RT "Whole genome shotgun sequence of Jishengella endophytica NBRC 109090.";
RL Submitted (AUG-2020) 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; AP023358; BCJ61475.1; -; Genomic_DNA.
DR EMBL; POTX01000013; PZG00118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2DK39; -.
DR KEGG; meno:Jiend_48970; -.
DR OrthoDB; 3182512at2; -.
DR Proteomes; UP000248627; Unassembled WGS sequence.
DR Proteomes; UP000682317; Chromosome.
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 371
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 418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 425..426
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 465 AA; 51134 MW; 15A3884A9DAA90AD CRC64;
MSDVIFPEGF VWGSATASYQ IEGAAKEDGR GPSIWDTYSH TPGRTLNGDT GDVAADHYHR
WADDLDQVAA LGLDAYRFSI AWPRVQPGGS GPVNQAGVDF YSRLVDRLLE LGIRPVATLY
HWDLPQELED AGGWPARDTA SRFVDYTEKI VGALGDRVHT WTTFNEPWCS AYLGYASGVH
APGRTEPAAA LAAVHHLNLA HGLAGRVIRE LAPAAQLSVT LNLHVIRPAS ESAADADAAR
RIDALANRAF LGPMLEGAYP ADLLADTAGV TDWSFVRDGD EQVAAVPLDV LGVNYYSTTL
VRAWDGVSPK SDSDGHGRSA HSAWVGSEQV EFLPQPGPHT AMGWNIEPAG LTELLLRLHR
EYPNQPMMIT ENGAAFADEV SPDGAIHDDR RIDYLRRHIA ATHDAMTAGA DVRGYFVWSL
LDNFEWGYGY DRRFGIIRVD YDTQQRTWKD SAHWYRTLTT TNRLP
//
