ID   A0A4Q7NNM8_9ACTN        Unreviewed;       810 AA.
AC   A0A4Q7NNM8;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, 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=EV189_2270 {ECO:0000313|EMBL:RZS86854.1};
OS   Motilibacter rhizosphaerae.
OC   Bacteria; Actinomycetota; Actinomycetes; Motilibacterales;
OC   Motilibacteraceae; Motilibacter.
OX   NCBI_TaxID=598652 {ECO:0000313|EMBL:RZS86854.1, ECO:0000313|Proteomes:UP000293638};
RN   [1] {ECO:0000313|EMBL:RZS86854.1, ECO:0000313|Proteomes:UP000293638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45622 {ECO:0000313|EMBL:RZS86854.1,
RC   ECO:0000313|Proteomes:UP000293638};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (FEB-2019) 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:RZS86854.1}.
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DR   EMBL; SGXD01000003; RZS86854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q7NNM8; -.
DR   OrthoDB; 3187421at2; -.
DR   Proteomes; UP000293638; 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   PANTHER; PTHR30620:SF16; LYSOSOMAL 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000293638}.
FT   DOMAIN          702..771
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   810 AA;  84583 MW;  C1EF5911350984A6 CRC64;
     MTSVPPETAT SATAAPRPWQ DPSRSAAERV ELLLAEMTLE ERVAQLGSRW VGNDMQEEHA
     PGDGAEDAET INVAPMQDVF AKSGTIPLDE ASRHGLGQLT RVYGSNPLSV AEGVAELVRQ
     HRVVLEGSRL GVPALVHEEC LTGFTTYGAT VYPAAIAWGA TFDPGLVERM AAAIGRDMAA
     VGVHQGLSPV LDVVRDYRWG RVEETIGEDP YLVAQLGAAY VRGLQSAGVI ATLKHFAGYS
     ASRAARNHGP VSMGRRELLD VILPTFEAAV ALGGARSVMN SYSDVDGVPA GADPWLLTQV
     LREDWGFTGT VVSDYWAVPF LATMHRVAAD YDAAGALALT AGIDVELPDT LGFGEGLVAL
     VRKGEVPEEL VDRAVRRVLL QKAELGLLDA DWTPEGSVAD AARDLDSAEN RAIARELAER
     SVVLLDAGSA LPLLGEGRPA LSRVAVVGPC ADDPRTFMGC YAFPNHVLPR HPELGLGLEV
     TTALAALRDE LPGVEVVHAA GCAVTGTDRS GIAEAVEAAR GADLAVAYVG DLAGLFGHGT
     SGEGCDADDL RLPGVQADLL DALLETGTPV VVVVVSGRPY ALGDVAPRAA GLVQAFMPGE
     EGGGALAGVL SGRTNPGGKL PVQVPRTVGG QPSTYLQPPL GGPESEGISN LDARPLFPFG
     FGASYTSFEV ADLALSSEQL ASDGEVTVTV RVANTGSRAG DEVVQLYASD PVAQVARPVR
     LLTGFARVTL EPGASAEVEF RVHADRFAYT GPDLRRIVEP GEVELLVGTS AAHLPCSGTV
     RVTGPTRVVG HDRRLDTPVT LRPVPTTPAG
//