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Database: UniProt
Entry: A0A1E7RID0_9GAMM
LinkDB: A0A1E7RID0_9GAMM
Original site: A0A1E7RID0_9GAMM 
ID   A0A1E7RID0_9GAMM        Unreviewed;       844 AA.
AC   A0A1E7RID0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BIY45_18585 {ECO:0000313|EMBL:OEY99121.1};
OS   Stenotrophomonas sp. BIIR7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1904462 {ECO:0000313|EMBL:OEY99121.1, ECO:0000313|Proteomes:UP000175905};
RN   [1] {ECO:0000313|EMBL:OEY99121.1, ECO:0000313|Proteomes:UP000175905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIIR7 {ECO:0000313|EMBL:OEY99121.1,
RC   ECO:0000313|Proteomes:UP000175905};
RA   Sanchez-Castro I., Ruiz-Fresneda M.A., Bakkali M., Kampfer P., Busse H.J.,
RA   Lopez-Fernandez M., Martinez-Rodriguez P., Merroun M.L.;
RT   "Stenotrophomonas bentonitica sp. nov., isolated from bentonite
RT   formations.";
RL   Submitted (SEP-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|ARBA:ARBA00000448};
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:OEY99121.1}.
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DR   EMBL; MKCZ01000131; OEY99121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7RID0; -.
DR   STRING; 1904462.BIY45_18585; -.
DR   Proteomes; UP000175905; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR041443; Exop_C.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF18559; Exop_C; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175905};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..844
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009201581"
FT   DOMAIN          60..385
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          422..639
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          672..829
FT                   /note="ExoP galactose-binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF18559"
SQ   SEQUENCE   844 AA;  89238 MW;  00DF3D6E0A97F152 CRC64;
     MSVSSARKTV LALCVLTALA AQAPAVSAAE RLQDWPRVTS AIAADPAIEA RVRTIVGQMT
     LAQKIGQMTQ PEIKQITPEQ VRTYYIGSVL NGGGSWPGMD KHASVADWVK LADAYHAASL
     STDARTPVPV IWGTDAVHGH SNVYGATLFP HNIGLGATRD AALIERIGAA TGTATRATGI
     GWVFAPTLAV AHDPRWGRTY ESFSSDPAVV REFATAYVKG AQGRFTADGN VVATAKHYIG
     DGATDNGRDQ GESTVDKATM INVHGQGYFG ALGEGVQTVM ASFNSWNDRA GGVDYGKMHG
     SQVLLTGALK DKMGFDGFVV SDWNGIAQVP GCRNDSCAQA INAGIDMVMV PDDWKAFIAN
     TMAQVESGEI PMARIDDAVT RILRVKLRAG LFDHKPSDSQ FAGDSAAVQH RELAREAVRE
     SLVLLKNQDA VLPLKRNARV LVVGESADNL SNQAGGWSLT WQGTENTNAD FPNADSVLGA
     LRAELGAAQV TFNADAKDID ATQFDVVVAV IGETPYAETN GDILASDTVS HSRAQPKDLA
     VLKAAAASGK PVVTVYFSGR PMYTNDLLNL SQGFVAAWLP GSEGKGITDV LVAGKDGKAA
     HDFTGRLSFP WPGVPCPAPI DRPDPKRPPL FTFGYGLSYA QPAQVARLPE VNADHCGEVT
     TLPIFNRLDT APFSLHIAAN GATQPLGNDL NASLRWPKEK PVAEVRTVQI NTQQDAREVT
     WLAPAQLIAR STSRRNLSAL ARSNGALQFD VMVQHQPASA VKVTMQCGTG CEGGVDIAST
     LASLQPGQKR TVTIPLACFA SKGVDLGAVE APFVVTADKP FAAAFTQVRV AAKADKAEGV
     VACR
//
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