ID A0A2V2Q599_9ACTN Unreviewed; 475 AA.
AC A0A2V2Q599;
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=DKT74_17120 {ECO:0000313|EMBL:PWS43368.1};
OS Streptomyces sp. ZEA17I.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS43368.1, ECO:0000313|Proteomes:UP000245984};
RN [1] {ECO:0000313|EMBL:PWS43368.1, ECO:0000313|Proteomes:UP000245984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZEA17I {ECO:0000313|EMBL:PWS43368.1,
RC ECO:0000313|Proteomes:UP000245984};
RA Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT "Genome sequencing and identification of chitinase family genes of
RT Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL Submitted (MAY-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|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:PWS43368.1}.
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; QGMS01001144; PWS43368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2Q599; -.
DR Proteomes; UP000245984; 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}.
FT REGION 447..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 361
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 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 409..410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 475 AA; 51904 MW; 4DC6F704088EDEBD CRC64;
MPVPQFPPGF LWGASASAFQ TEGAVDADGK GPSGWDAFAA LPGRIKDGTD TTRATGFHDR
YREDVALLAG LGADAFRFSV SWPRVVPGGS GAVNADGLDF YDRLVDELCA HGITPAPTLY
HWDTPLPLEE AGGWLDRDTA YRFAEYAGIV AERLADRVPM WITINEPAEV TLLGYALGEH
APGRTLLFDA LPAAHHQLLA HGLAVRALRA AGADNIGAAF SHAPVWTAGD ADEDRFGAEL
YDTLTNWLFA DPVLTGRYPD DGLAALMPGP VADDLKVIST PLDWYGVNYY NPTLVGAPRP
EALETFSGFA MPAELPFGIR EIEGYEKTGF GWPVVPEGLT EILTLLHRRY GDRLPPLHIT
ENGCALAEPL ADDRRIAYLE SHLTALRAAM DAGVDVRGYF TWSLTDNVEW TEGASQRFGL
VHIDFETLAR TPKASYAWYR DLIRAQKRQK PDRMQQGRRK NRNPAVEGAY AAPSE
//
