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Database: UniProt
Entry: A0A0J1DC03_9BURK
LinkDB: A0A0J1DC03_9BURK
Original site: A0A0J1DC03_9BURK 
ID   A0A0J1DC03_9BURK        Unreviewed;       837 AA.
AC   A0A0J1DC03;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=AB595_12860 {ECO:0000313|EMBL:KLU36642.1};
OS   Massilia sp. WF1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU36642.1, ECO:0000313|Proteomes:UP000036336};
RN   [1] {ECO:0000313|Proteomes:UP000036336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA   Lou J., Gu H., Wang H., Xu J.;
RT   "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT   strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT   contaminated soil.";
RL   Submitted (JUN-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   -!- 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:KLU36642.1}.
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DR   EMBL; LELH02000012; KLU36642.1; -; Genomic_DNA.
DR   RefSeq; WP_047825279.1; NZ_LELH02000012.1.
DR   AlphaFoldDB; A0A0J1DC03; -.
DR   PATRIC; fig|1406431.3.peg.1529; -.
DR   Proteomes; UP000036336; 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:UP000036336};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..837
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005249676"
FT   DOMAIN          59..384
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          421..635
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          691..818
FT                   /note="ExoP galactose-binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF18559"
SQ   SEQUENCE   837 AA;  88145 MW;  0FE57363BBB378EE CRC64;
     MHKPLRFGAL AIAVALTLPA IGAEPVAEQK LTDWPHIASE FRKDPALEAR VAEILARMTL
     AQKIGQMTQP EIKSVTPDEV RKYYLGSVLN GGGSWPNNDK HARAADWLAM ANAFYDASMA
     TDMPIKVPVV WGTDAVHGHN NVYGATMFPH NIGLGAARDP ALIGEIGAAT AKAVRATGIA
     WVFGPTLAVV RDDRWGRTYE SYSEDPLLVK RYAGVYVKGM QDHFRKDYNT IATAKHFMGD
     GGTDQGKDRG VNKSTALDMM NIHAQGYYTA LAAGAQAVMA SFNSWDDVAA GKNYGKIHGS
     RDMLTGILKE KMGFDGFVVT DWNGHGEVPG CSAASCVQAI NAGVDMVMVT DEWKDFIKNT
     MADVEAGRIP MARIDDAVTR ILRVKLRAGL FGKRPSQNAY AGKDEALQAR GLARRAVRES
     LVLLKNEGPA LPLAAGKKLL VVGKAADSMA HQTGGWALTW QGTTNTNADF PNADTILAGI
     RAAAGAAEVS FSPDGKGVNP ADYDAVIAVI GEGPYAEGDG DIGPSGTLRH SSRYPEDLAV
     LQQVAGKGRP VVTVFLSGRP LWVNDLLNLS DTFVAAWLPG TEGKGVADLL VASKGGKALD
     FRGTLSFSWP KTVCQTPLNV GDPGYAPLFA YGYGLRKGMR SHLGQLDTTY PAGGCGSSQI
     YPLYGQADRA SFPLQLRSGA AVQPLGADLN ATVSLPGITV ATSQINTQQD AKMVTWSGPA
     SFEAHGAKPL ALPAAAAKDA ALRFDTIVQA APAGRVTVAM GGTALDATAL FGRLAGKGKQ
     AVKIPLACFT AKGLDLDKVD TPFSVSSTGA FAAAFGNIDA VGGAAGDQDA VRCEELR
//
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