ID A0A0N1NEX6_9ACTN Unreviewed; 463 AA.
AC A0A0N1NEX6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=OK006_5616 {ECO:0000313|EMBL:KPI08230.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI08230.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI08230.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI08230.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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|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:KPI08230.1}.
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DR EMBL; LJCU01000222; KPI08230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NEX6; -.
DR PATRIC; fig|1592326.3.peg.6849; -.
DR Proteomes; UP000037912; 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:KPI08230.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:KPI08230.1}.
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 418..419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 463 AA; 50929 MW; 992565DD18866738 CRC64;
MTDSSSPEGT SVTIDLAALP EDFLWGTATS AYQIEGAVAE DGRSPSIWDT FSHTPGKIDN
GDHGDIACDH YHRWREDIAL MRQLGTNAYR LSIAWPRVVP GGDGPVNAKG LDFYDQLIDA
LLEAGITPSV TLYHWDLPQV LQDRGGWPAR DTAHHFASYA AVVAERLGDR VQHWTTLNEP
LCSAWIGHLE GRMAPGLADL AVAVPASYHL LLGHGLAVQA IRAAAPGAQV GIVNNLSSVE
AATDRPEDVE AARRLDGHTN RWWLDPVHGR GFPADMREVY GIELPELPGD LETIAQPLDW
LGLNYYFPST VADDPSGPAP RVRTVRRLGV PRTGMDWEVD ASGIERLLLR LTDDYGARKL
YVTENGSAYP DVVRPDGTVD DPERTRYLEQ HLAACAAAAG KGVPLAGYFA WSLLDNFEWA
YGYDKRFGLV HVDYETQRRT VKGSGHRYAD IIRAHGERRR NAA
//
