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Database: UniProt
Entry: A0A0Q4Q567_9SPHN
LinkDB: A0A0Q4Q567_9SPHN
Original site: A0A0Q4Q567_9SPHN 
ID   A0A0Q4Q567_9SPHN        Unreviewed;       761 AA.
AC   A0A0Q4Q567;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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=ASE90_01890 {ECO:0000313|EMBL:KQN91577.1};
OS   Sphingomonas sp. Leaf67.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736230 {ECO:0000313|EMBL:KQN91577.1, ECO:0000313|Proteomes:UP000051342};
RN   [1] {ECO:0000313|EMBL:KQN91577.1, ECO:0000313|Proteomes:UP000051342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf67 {ECO:0000313|EMBL:KQN91577.1,
RC   ECO:0000313|Proteomes:UP000051342};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN91577.1, ECO:0000313|Proteomes:UP000051342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf67 {ECO:0000313|EMBL:KQN91577.1,
RC   ECO:0000313|Proteomes:UP000051342};
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:KQN91577.1}.
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DR   EMBL; LMLP01000001; KQN91577.1; -; Genomic_DNA.
DR   RefSeq; WP_055995179.1; NZ_LMLP01000001.1.
DR   AlphaFoldDB; A0A0Q4Q567; -.
DR   STRING; 1736230.ASE90_01890; -.
DR   Proteomes; UP000051342; 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}.
FT   DOMAIN          680..749
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   761 AA;  81206 MW;  0A38F8C9DB69DC76 CRC64;
     MEDIRISRRA IMMGAGAIAA WSASPARALL AQAGDRLPAS VEALVGQMTV EEKAGQLTLM
     AAAWAGGAAN ALNPIGATAT FDEQLAQVRA GRLTGVFNGN GADMARRMQT VAMKEQRLKV
     PLLFAADIIH GFRTVFPMPL AEAGTFDADL AERTARAAAV EASAAGIDWT FAPMVDIARD
     QRWGRGIEGA GEDLLLGKTM ADARVRGFQG RRGLMADDAV AACAKHFAAY GAGEAGLDYN
     TVDVSERTLR ETYFPPFQTA FAAGAPTTMA SFNELSGVPA TANPWLLDTI LRKEWGFGGL
     VVSDYTGDEE LIAHGFAADA REATKLAFLA GVDMSMQSGF YLKHLPDLVA KGEVPMERLD
     QAVRRVLALK VQLGLFDNPF RRIDPRREKQ RVRTAAHLKL AREAGARSIV MLKNDGDLLP
     LPKSGKRIAL IGPFVQGQRE LIGTWNVYGS DAEAVDLLTG VRAAVTDPRM VTAVDGSGIT
     DPIPGGIEAA VIAASQADIV LLAIGESQRM SGEAQSRVDI GIPRAQLDLA EAVLATGKPT
     VLLLRNGRAM VLDKPVLDAR AILVTWFLGS ESGPATADIL FGDVGPSARL PVSFPYATGQ
     QPYYYAHKAT GRPNPPGPLA EYKARYREGP NAARFPFGHG LTYGRIAYSD LDLGDGRLNS
     DGALKVRARV TNSGTRAATE VVQLYIHDVA ASITRPVREL KAFQRVTLAP GESKVVEFTL
     RANDLRFIGV ENRPVVEPGS FHVWVAPSAE ADGVNGSFVL A
//
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