ID A0A1L3MUK6_9BACI Unreviewed; 449 AA.
AC A0A1L3MUK6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=A9C19_15455 {ECO:0000313|EMBL:APH06022.1};
OS Bacillus weihaiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH06022.1, ECO:0000313|Proteomes:UP000181936};
RN [1] {ECO:0000313|EMBL:APH06022.1, ECO:0000313|Proteomes:UP000181936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alg07 {ECO:0000313|EMBL:APH06022.1,
RC ECO:0000313|Proteomes:UP000181936};
RX PubMed=27901120; DOI=10.1038/srep38248;
RA Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT "Complete genome sequence and transcriptomic analysis of a novel marine
RT strain Bacillus weihaiensis reveals the mechanism of brown algae
RT degradation.";
RL Sci. Rep. 6:38248-38248(2016).
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|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR EMBL; CP016020; APH06022.1; -; Genomic_DNA.
DR RefSeq; WP_072580823.1; NZ_CP016020.1.
DR AlphaFoldDB; A0A1L3MUK6; -.
DR STRING; 1547283.A9C19_15455; -.
DR KEGG; bwh:A9C19_15455; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000181936; Chromosome.
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; IPR018120; Glyco_hydro_1_AS.
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; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000181936}.
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 ECO:0000256|PROSITE-ProRule:PRU10055"
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 449 AA; 52182 MW; E0DC61E0C77B1066 CRC64;
MTRFSKDFIF GTATSSYQIE GAWNEDGRTA SIWDEFSSIP GKVWNMDNGN IACDHYHRYE
EDVEILKTLG VDSYRFSIAW PRIFPEKGKY NPDGMEFYKK LISLLHSANI KPAVTLYHWD
LPMWAHEQGG WTNRESVKWF MEYAEKCFEE LDDQVDMWIT HNEPWCAGFL GYHQGVHAPG
HKNMEEALKA VHHILLSHGE AVDYLKNKRQ STTPIGITLN LSPVYPASDS MNDQLAANNA
DGYTNRWFLD PIFKGNYPLD MMNLFSKYVH DYSFIKEGDM KKISIECDFF GINYYNRSLV
EFTSASDFLF TSAYSDYDKT GMGWDISPNE FKQLIHRLRQ EYTTLPIYIT ENGAAFDDTV
APDGKVYDVG RESYVEKHIT AVAELNEDNM NIAGYYLWSL LDNFEWAFGY DKRFGITYVD
FLTQKRTLKN TGFRYAEIIK NRSLEKILI
//
