ID A0A418KLQ7_9ACTN Unreviewed; 457 AA.
AC A0A418KLQ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=DY240_20535 {ECO:0000313|EMBL:RIQ18865.1};
OS Jiangella rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Jiangella.
OX NCBI_TaxID=2293569 {ECO:0000313|EMBL:RIQ18865.1, ECO:0000313|Proteomes:UP000284057};
RN [1] {ECO:0000313|EMBL:RIQ18865.1, ECO:0000313|Proteomes:UP000284057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY265 {ECO:0000313|EMBL:RIQ18865.1,
RC ECO:0000313|Proteomes:UP000284057};
RA Han C.;
RT "Isolation, diversity and antifungal activity of actinobacteria from
RT wheat.";
RL Submitted (SEP-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:RIQ18865.1}.
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DR EMBL; QUAL01000186; RIQ18865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418KLQ7; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000284057; 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, ECO:0000313|EMBL:RIQ18865.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:RIQ18865.1}.
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 164
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 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 410..411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 457 AA; 50378 MW; 7430EE8E2F7E9CE1 CRC64;
MTFRFPPEFL WGAATSAYQV EGSLDVDGRG ESVWDVFARQ PGSIEGGGDG SLACDSYRRW
ADDVELIASL GLNAYRFSVG WSRVMPDGRG RVEKRGLDHY ERFVDALLDR GVTPVLTLNH
WDMPQALMSD GGWVARSSVD AFAEFTAAVA DRLADRVEWW VTQNEPWIIA LLGYQLGLHA
PGVRDLGASV TAGHHVLLAH GAGADILRQY PRTRAGVALS LFPCDPATPS EEDAAAAWGS
DGYVNRWYLD PLAGRGYPAD MREHYERALG RPLTEIRDGD EDAIAGRSDF LGVNYYTRRV
MAAAEPGKGR PFPWRVVGPS GDVARTDEGW EIAPGSFRDL LLRLHRDYGF PLLVTENGGV
FGDAPLHDGR VRDVRRQAFL HSHVAAMGEA MAAGADVRGY LHWSLLDNFE WSLGYRPRFG
LVHVDYPTGR RTVKDSGRLY ARIVAAGTTD VEESEDA
//
