ID A0A0A8X5Z5_9BACI Unreviewed; 444 AA.
AC A0A0A8X5Z5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMD00020551_2583 {ECO:0000313|EMBL:GAM14432.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM14432.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM14432.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM14432.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-2013) 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:GAM14432.1}.
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DR EMBL; BASE01000056; GAM14432.1; -; Genomic_DNA.
DR RefSeq; WP_041966188.1; NZ_BASE01000056.1.
DR AlphaFoldDB; A0A0A8X5Z5; -.
DR STRING; 1321606.SAMD00020551_2583; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000031014; 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, ECO:0000313|EMBL:GAM14432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031014}.
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 351
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 405..406
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 444 AA; 51430 MW; F44D7266CAE08233 CRC64;
MTRFSRDFIF GTATSSYQIE GAYQEDGRSL SIWDTFSRTP GKVFNMDNGD IACDHYHLYE
KDIEILKTLG VDSYRFSIAW PRIFPEQGKF NEAGMNFYKK LIARLIESGI KPAVTLYHWD
LPMWAHEKGG WTNRESVDWF MEYAEKCFEE LDEHVEMWIT HNEPWCAGFL GYHQGVHAPG
HTNMEEALKA VHHILLSHGE AVSLLKGKFA SATPIGITLN LSPVYPASNS ANDRLAANNA
DGYTNRWFLD PVLKGSYPVD MMNLFSKYVH SFDFIQEGDL EKISIECDFF GINYYNRSLV
EFNAASDFLF MSAYSDYSKT GMGWDISPSE FKELIHRLRK EYTNLPIYIT ENGSAFDDQV
SDDHRVHDSE RQDYVEKHIW AVAELNEEGM NIAGYYLWSL LDNFEWAFGY DKRFGITYVD
FETQERILKD SGYRYAEIIS NRSI
//
