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Database: UniProt
Entry: A0A0M8VPF2_9ACTN
LinkDB: A0A0M8VPF2_9ACTN
Original site: A0A0M8VPF2_9ACTN 
ID   A0A0M8VPF2_9ACTN        Unreviewed;       471 AA.
AC   A0A0M8VPF2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=ADL00_10435 {ECO:0000313|EMBL:KOV69959.1};
OS   Streptomyces sp. AS58.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV69959.1, ECO:0000313|Proteomes:UP000037758};
RN   [1] {ECO:0000313|EMBL:KOV69959.1, ECO:0000313|Proteomes:UP000037758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS58 {ECO:0000313|EMBL:KOV69959.1,
RC   ECO:0000313|Proteomes:UP000037758};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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|RuleBase:RU361175};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {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:KOV69959.1}.
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DR   EMBL; LGDU01000070; KOV69959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8VPF2; -.
DR   PATRIC; fig|1519489.3.peg.2415; -.
DR   Proteomes; UP000037758; 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:InterPro.
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; LACTASE-LIKE PROTEIN; 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   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:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037758}.
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        369
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         416
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         423..424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   471 AA;  52203 MW;  E37E8F0D30488DB0 CRC64;
     MPEFSGFPAF PDGFFFGAAT ASYQIEGAYD EGGRGPSIWD TFSREPGRVV GGATGDVACD
     HYHRYPEDVA LLRNLGVDSY RFSIAWPRIQ PTGSGPANKA GLDFYDRLLD ELHAAGISPA
     ATLYHWDLPQ ALEDRGGWRV RETAERFAEY TAIVADRFGD RVDRWITLNE PFCSAFVGYA
     AGGHAPGTRE GRGALAAAHH LLVGHGLAVR ALRAAGAKEV GITLNPDRLL PATESAADLA
     AVRRAETMHN DVWFEPIFAG RYPQHEAETW GELLDSGEPY RQEGDLELIG APLDFVGINY
     YRPITVSDAP HEDPDPASRS AVDIRAVESW RADVRHTTMG WPVVPHTFTD LLVDLAKRYP
     TLPPVLITEN GSAEADSVDA EGRVRDTDRV EYLRTHLEAL ATAMQAGVDV RGYYVWSLLD
     NFEWARGYDQ RFGIIRVDYD TLERTPKDSY HWYRQLIADH RARTGGADPA E
//
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