ID A0A2B2CBH1_9BACI Unreviewed; 447 AA.
AC A0A2B2CBH1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=COJ96_10345 {ECO:0000313|EMBL:PFP29534.1};
OS Bacillus sp. AFS073361.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP29534.1, ECO:0000313|Proteomes:UP000223997};
RN [1] {ECO:0000313|EMBL:PFP29534.1, ECO:0000313|Proteomes:UP000223997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS073361 {ECO:0000313|EMBL:PFP29534.1,
RC ECO:0000313|Proteomes:UP000223997};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PFP29534.1}.
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DR EMBL; NUZU01000015; PFP29534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B2CBH1; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000223997; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000223997}.
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 353
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 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 406..407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 447 AA; 51857 MW; 852E93DC28FACF86 CRC64;
MSIITFPKDF RFGVSTAAYQ IEGAYNEDGR GMSIWDTFSR IPGKVRNGDN GDIACDSYHR
IDEDIALLKE LGVNTYRFSI AWPRIFPNGR GEVNQKGLDH YHTFVDKLLE NGIEPLCTIY
HWDLPQALQD EGGWKNRQTI EAFVEYSDLL FHEFSGKIKS WLTINEPWCV SFLGYFIGEQ
APGEKNLQSA LDVAHHLLLA HGKTVKRFKE LGIPGEIGFA PNVTWYEPFS DRPEDIEACK
RISAWFTEWF FDPVFKGSYP QILVDWFAAK GAKVNIEEGD MELINQPIDI LGINYYTGTV
SRYKEGQGTF DCEHIDIGFD HTDIDFTIYP EGFYKVLMDI KNKYGDVPIY ITENGATYNQ
DPIDGRVRDD KRIKYLKQHL TQISRALNSG VNLKGYCIWS LMDNYEWSYG YSMRFGLVHV
DYQTLNRTKK DSYYWYSKLN QNYWFEV
//
