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Database: UniProt
Entry: A0A0W1QN52_9SPHN
LinkDB: A0A0W1QN52_9SPHN
Original site: A0A0W1QN52_9SPHN 
ID   A0A0W1QN52_9SPHN        Unreviewed;       817 AA.
AC   A0A0W1QN52;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=ATB93_06615 {ECO:0000313|EMBL:KTF69939.1};
OS   Sphingomonas sp. WG.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF69939.1, ECO:0000313|Proteomes:UP000052965};
RN   [1] {ECO:0000313|EMBL:KTF69939.1, ECO:0000313|Proteomes:UP000052965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WG {ECO:0000313|EMBL:KTF69939.1,
RC   ECO:0000313|Proteomes:UP000052965};
RA   Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT   "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT   strain.";
RL   Submitted (NOV-2015) 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:KTF69939.1}.
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DR   EMBL; LNOS01000021; KTF69939.1; -; Genomic_DNA.
DR   RefSeq; WP_019369857.1; NZ_LNOS01000021.1.
DR   AlphaFoldDB; A0A0W1QN52; -.
DR   Proteomes; UP000052965; 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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KTF69939.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052965};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..817
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006927217"
FT   DOMAIN          62..387
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          424..637
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          673..805
FT                   /note="ExoP galactose-binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF18559"
FT   REGION          26..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  84826 MW;  A59FDCC4C93883EB CRC64;
     MPAGLKLLLA TTILAAAPAV AQQAPTTLSS TAHPEKWPAA KTPGLIDPAT EKSITDLLAK
     MTLEEKVGQM IQADIGSITP ADLATYPLGS ILAGGSSPPI GAPDRSPRGP WLATAQAFQK
     AALARKGNHA AIPIMFGIDA VHGNNNIVGA TLFPHNVGLG AMRDPALMEK IGRATAAETA
     SAGIDWAFGP TLAVPQDDRW GRAYEGYSED PEVVRSYAGA MIRGLQGAPG TKDRIQKGYV
     AASAKHFLGD GGTFGGQDQG DTRVSEEELI RIHNAGYPGA INAGTMTVMA SFSSWNGAKM
     HGNKSLLTDV LKGKMGFDGF VVGDWNGHAQ IPGCTATDCA ATFNAGLDMA MAPDSWKGLY
     ESTLAHAKAG TIPMARIDDA VRRILRVKMQ MGLFEAARPY ESKAEIIGAP EHRAIAREAV
     AKSLVLLKNN GVLPLKASAN VLVAGSGADS MAQQSGGWTL SWQGDGNPNA MFPNGETIFA
     GIQAAVKAGG GTATLSADGS FTKKPDVAIV VFGEEPYAEM RGDVRTLEFQ PGDKQALALL
     KKLKAAGVPV VSVFLSGRPL WVNPELNASD AFVAAWLPGS EGAGVADVLI GDKAGKPRRD
     FTGTLSFSWP KTAGQFTLNR GAAGYDPLFA FGYGLRYAKP GTVGTLSEVS GVDAALGNTG
     TFFAKGVTPA PFSFATDSGV TRKTVDGPAT QEGAQQLTWP AGPATLRIGG GDLDLSRETN
     GDLSLRLVYR VDAAPTGPVR LSMEGGTNTG TIDATGLFTG KTGWQTVNVL LKCYQKNGVD
     VTKVNAPIVL QASGPFTLSL AEARIVSDPA NSVCPGQ
//
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