ID   A0A369VX93_9SPHN        Unreviewed;       757 AA.
AC   A0A369VX93;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=DVW87_00225 {ECO:0000313|EMBL:RDE06207.1};
OS   Sphingomonas aracearum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2283317 {ECO:0000313|EMBL:RDE06207.1, ECO:0000313|Proteomes:UP000253918};
RN   [1] {ECO:0000313|EMBL:RDE06207.1, ECO:0000313|Proteomes:UP000253918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WZY 27 {ECO:0000313|EMBL:RDE06207.1,
RC   ECO:0000313|Proteomes:UP000253918};
RA   Zhiyong W., Qinglan Z., Zhiwei F., Ding X., Gejiao W., Shixue Z.;
RT   "a novel species of Sphingomonas isolated from the rhizosphere soil of
RT   Araceae plant.";
RL   Submitted (JUL-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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:RDE06207.1}.
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DR   EMBL; QQNB01000001; RDE06207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369VX93; -.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000253918; 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; 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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
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   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253918};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..757
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016605321"
FT   DOMAIN          676..745
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   757 AA;  79753 MW;  8FAE50C099820D90 CRC64;
     MTDTRITRRA ALMAAGAIGA WAASPARALL RSTDATASPD LDALVSRMTI EEKAGQLTLN
     AAAWAGSAAT ALNPPSAGAT FTEQLAQVRA GHLTGVFNGN GAEMSRQMQL AAIKQSRLKI
     PLIFAADIIH GFRTIFPVPL GEAASWDPEL AERTARIAAV EAAAAGIDWT FAPMVDIARD
     QRWGRGVEGA GEDVWLGKMF AAARVKGFQG DKLTAADAVM ACMKHFAAYG AAEAGLDYST
     VDVSERTLRD VYLPPFKTGL DAGALSVMAA FNELSGIPAT ANDWLMRTVL RDEWKFDGIV
     VSDYTGDEEL IAHGVAKDGR DAARLAFLAG VDMSMQSGLY MQHLPGLVAA GEVPMARVDE
     SVRRVLAVKA RLGLFDDPFR RIDPRREKTR VLTPAHRKVA REAAVKSAVL LKNEGNLLPL
     PKSGKRIALI GPFAEGKHDL VGPWCVYGDD AQAVDLATGL RAKGATITVT QGCAPEEAIA
     GGIEAAVAAA RAADVVVLAV GEHTGMSGEA QARASIALPD PQLALAEAVA GTGKPIVVVL
     KNGRALELAG AIANAPAILV TWFLGSETGN AIADLLFGDA SPSGRLPVSF PHATGQQPYY
     YAHKPTGRPN PPGAPQAYKA HFRGILNDAL YPFGHGLTYG QIGYSALQLG GGRLPANGQL
     AVQATLTNNG ARAAEEVVQL YIRDRVASVT RPVRQLVNFR RVALAPGASQ QVRFTITPQD
     LAFIGRDLKS VVEPGTFDVW IAPSAEAEGV HGTFELG
//