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Database: UniProt
Entry: A0A433Y5I5_9BACL
LinkDB: A0A433Y5I5_9BACL
Original site: A0A433Y5I5_9BACL 
ID   A0A433Y5I5_9BACL        Unreviewed;       450 AA.
AC   A0A433Y5I5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=EJP82_19320 {ECO:0000313|EMBL:RUT43849.1};
OS   Paenibacillus anaericanus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=170367 {ECO:0000313|EMBL:RUT43849.1, ECO:0000313|Proteomes:UP000279446};
RN   [1] {ECO:0000313|EMBL:RUT43849.1, ECO:0000313|Proteomes:UP000279446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15890 {ECO:0000313|EMBL:RUT43849.1,
RC   ECO:0000313|Proteomes:UP000279446};
RA   Sun L., Chen Z.;
RL   Submitted (DEC-2018) 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|ARBA:ARBA00010838, 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:RUT43849.1}.
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DR   EMBL; RZNY01000017; RUT43849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433Y5I5; -.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000279446; 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; 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, ECO:0000313|EMBL:RUT43849.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279446}.
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        355
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10055"
FT   BINDING         17
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         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         409..410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   450 AA;  51818 MW;  66ED0FDC8F35C5CC CRC64;
     MSFNSNFVWG AATAAYQIEG AASEDGKGLS VWDMCAHIPS FVKGNHTGDH ACNHYYRYKE
     DVQLMKEIGL QAYRLSISWP RVLPDGTGRI NEKGLDFYDR LIDELLENGI TPYVTLFHWD
     YPHELFKKGG WLNPDSSDWF AEYTRVIADR LSDRVTNWFT QNEPQCYIGL GHSNGTHAPG
     LKLGQAEVLQ ATHNSLLAHG KAVQTLRQYS KQPCQIGYAP VGITSFPETE TPENIEAARR
     HTFSITEPTF WMNTWYMDPV FLGHYPEDGL KVFEPWLPTI KPGDMETINQ PLDFLGLNIY
     HGTPVKMGAD SKPQLIGNHD GYPQTSMRWT VTPESLYWGP KFFYERYGAP IVITENGMAN
     LDWVNLDKQV HDPQRIDYMH RYLQEYRRAA TDGVDVKGYF YWSFMDNFEW AEGYNERFGL
     VHTDYRDGKR TIKDSGYWYR SVIQSNGESL
//
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