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Database: UniProt
Entry: A0A257CBJ1_9BURK
LinkDB: A0A257CBJ1_9BURK
Original site: A0A257CBJ1_9BURK 
ID   A0A257CBJ1_9BURK        Unreviewed;       461 AA.
AC   A0A257CBJ1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=CFE46_14980 {ECO:0000313|EMBL:OYT86753.1};
OS   Burkholderiales bacterium PBB6.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015568 {ECO:0000313|EMBL:OYT86753.1, ECO:0000313|Proteomes:UP000216978};
RN   [1] {ECO:0000313|EMBL:OYT86753.1, ECO:0000313|Proteomes:UP000216978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB6 {ECO:0000313|EMBL:OYT86753.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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:OYT86753.1}.
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DR   EMBL; NKIH01000005; OYT86753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257CBJ1; -.
DR   Proteomes; UP000216978; 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|RuleBase:RU361175};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216978}.
FT   ACT_SITE        173
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         27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         301
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   461 AA;  50804 MW;  1544069CE6BEBCDE CRC64;
     MTTPTPTDPT LQFPPEFVWG VATSAFQIEG AADVDGKGPS IWDTFCQQPG AIADASDGRI
     ACDHYHRWES DLDLIADLGV DAYRFSVSWP RVRPGGSGAW NPRGLGFYER LVDGLLARGL
     KPYVTLNHWD LPDELQANGG WANRDTVHRF VEYAQGLADC LGDRVASITT HNEPWVMSVL
     GHETGIFAPG VKNRATAMQA SHHLLLSHGL AIQALRAQSV KAQLGIVLNL SPMHAATAAP
     ADLAKARLED GRLTRWFLDP IFNASYPADV LEALGADAPR VEAGDMNAIA SRMDFLGVNY
     YSRAVVSADG PWDVSRSGRE ITDMGWEIYP EGLTELLMRL QRDYPVPPLF VTENGGAFKD
     SLVDGRVHDR QRTDYIARHI AAVAEAMRQG VRMGGYMVWS LMDNFEWASG YEKRFGIVHV
     DYETQARTLK DSARWYREFL HRQKADSSAT TLPSAGSVTG A
//
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