ID A0A1H0V9M0_9ACTN Unreviewed; 478 AA.
AC A0A1H0V9M0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN04487981_13727 {ECO:0000313|EMBL:SDP75044.1};
OS Streptomyces sp. cf386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDP75044.1, ECO:0000313|Proteomes:UP000198720};
RN [1] {ECO:0000313|Proteomes:UP000198720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNHV01000037; SDP75044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0V9M0; -.
DR STRING; 1761904.SAMN04487981_13727; -.
DR Proteomes; UP000198720; 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:UP000198720}.
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 378
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
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 310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 432..433
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 478 AA; 52386 MW; 459F3F2C5178E966 CRC64;
MASPSCTTVT AATAMGGFPK LPAGFRFGAA TSAYQIEGAH DEDGRGPSVW DTFSHTPGRT
HAGATGDVAA DHYHRHREDV ALLRDLGVDS YRFSIAWSRL LPQGVGPVNP KGLDFYDRLI
DDLLAAGVAP AVTLYHWDLP QALEDRGGWR VRETAEAFAA YAALAAERYG DRVERWITLN
EPYCSAFVGY AEGRHAPGAR EGRGALAAAH HLLLGHGLAV SALRASRARE IGITLNLDRI
HAASDRPEDR AALRRAETLH NDIWTEPLFA GRHPRDEAET WAGLADGPWR LPGDLDLIGI
PLDFVGLNFY RPLTVAAAPH QAADPEQRTA VDVGVAELDP YGTRHTTMGW PVVPSAFTEL
LRDLHARYPQ LPPIWITENG SAEADTVSPD GRIHDPARIA YLADHLAAVA DAVAAGVDVR
GYYAWSLLDN FEWARGYDQR FGLVHVDYAT LTRTPKDSYH WYRRLITAHR AGTEEPAR
//
