ID A0A1H0PJX9_9BACI Unreviewed; 449 AA.
AC A0A1H0PJX9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=SAMN05216565_101334 {ECO:0000313|EMBL:SDP04896.1};
OS Litchfieldia salsa.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Litchfieldia.
OX NCBI_TaxID=930152 {ECO:0000313|EMBL:SDP04896.1, ECO:0000313|Proteomes:UP000199159};
RN [1] {ECO:0000313|Proteomes:UP000199159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10078 {ECO:0000313|Proteomes:UP000199159};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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|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; FNJU01000001; SDP04896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0PJX9; -.
DR STRING; 930152.SAMN05216565_101334; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000199159; 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; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
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.
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:UP000199159}.
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 ECO:0000256|PROSITE-ProRule:PRU10055"
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 449 AA; 52130 MW; DEF7E026B66B0155 CRC64;
MAIIEFPKDM KWGAATASYQ VEGGAFEDGR GASIWDTFSR TPGKVLNGDN GDVACDTYHR
YEEDIKLMKE LGIDSYRFSV AWPRIFPNGR GEVNQPGVDF YHRFVDTLLE NGIEPMCTLY
HWDLPQALQD EGGWANRSTI DAFVEYSEFM FKEFQGKIKN WITLNEPWCV SFLSNFIGEH
APGNKDLQLA TDISHHLMVA HGRSVKAFRT LKIDGQIGYA PNVTWKEPFS NKQEDIDACK
REVGWFVEWF MDPVFKGSYP QFMVDWFESK GVKMNIQDGD LQDISQPIDF LGINYYTGNV
ARYKENSGLF DSEDLDMNYE RTDIGWPIYP EGFYKVLTYI TELYGQVPIY ITENGACYND
EAENGRVKDQ RRITYLQLHL AALKRSMDSG VNIKGYLTWS LMDNFEWAFG YSMRFGIVHV
DFRTLVRTKK DSYYWYKQTL ENGWFDLTY
//
