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Database: UniProt
Entry: A0A0Q5Q2S3_9SPHN
LinkDB: A0A0Q5Q2S3_9SPHN
Original site: A0A0Q5Q2S3_9SPHN 
ID   A0A0Q5Q2S3_9SPHN        Unreviewed;       765 AA.
AC   A0A0Q5Q2S3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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=ASG07_03455 {ECO:0000313|EMBL:KQR87929.1};
OS   Sphingomonas sp. Leaf343.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR87929.1, ECO:0000313|Proteomes:UP000051323};
RN   [1] {ECO:0000313|EMBL:KQR87929.1, ECO:0000313|Proteomes:UP000051323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf343 {ECO:0000313|EMBL:KQR87929.1,
RC   ECO:0000313|Proteomes:UP000051323};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR87929.1, ECO:0000313|Proteomes:UP000051323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf343 {ECO:0000313|EMBL:KQR87929.1,
RC   ECO:0000313|Proteomes:UP000051323};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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, 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:KQR87929.1}.
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DR   EMBL; LMPG01000001; KQR87929.1; -; Genomic_DNA.
DR   RefSeq; WP_055842166.1; NZ_LMPG01000001.1.
DR   AlphaFoldDB; A0A0Q5Q2S3; -.
DR   STRING; 1736345.ASG07_03455; -.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000051323; 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:UP000051323};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..765
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006259405"
FT   DOMAIN          682..751
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   765 AA;  81117 MW;  C54ED326F57F6FC2 CRC64;
     MVDTRLSRRA ALMGAGAVAA WASSPARALL MQADATIRMG VVPAPVDALI ARMTLEEKAG
     QLTLNAAAWG GGVATALNPP STGPSFEGQV ADAVAGKLTG VFNGNGAVMA ERMQRAVMQG
     SRLKIPLIFA ADVIHGHRTI FPVPVAEAAS FDPDLAMRTA RVAASEAAGA GIDWTFFPMV
     DIARDQRWGR TMEGAGEDVR LGELFAAARV RGFQGRDLKA DDAMMACIKH FAAYGAAESG
     LDYNVVDLSE RTLREVYLPP YKAGFDAGAM SAMASFNEIA GIPATGNPWL MKTVLRDEWR
     FPGIVVSDYT GDEEMIAAGF AEDGRDAARI AFMAGVDMSM QSNLYMLHLP GLVREGLVPQ
     ATLDASVRRV LAVKHMLGLF DDPFRRIDVK REKARSRTRA NLALSREAAR RSIVLLKNDG
     GLLPLPTSGK RIALIGPFAS GQHDLNGPWV VYGDNANAVD LATGIRGALK DQNALTVVAG
     CDVEKPIPGG IEAAVAAARA ADIVLLAIGE NEGMSGEAQS RTEIVVPAPQ QALAEAVAAT
     GKPVVIVLKN GRALALTGVV RDAPAILVTW FLGSESGNAT ADILFGTASP SGRLPMSFPF
     ESGQEPYHYD HKATGRPAQA LSDTYKAKYR TALNAALYPF GHGLTYGTIG YSALSLPPTM
     AWNGVIEIAA TVTNTGARTA EETVQLYIRD RVATITRPVR EMKAFRKVRL APGAGETVRF
     TLKRSDLEFI GVDMKPTVEA GEFDVWIAPS AQAEGVTGRF VLAAG
//
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