ID A0A0Q5USE1_9SPHN Unreviewed; 790 AA.
AC A0A0Q5USE1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ASG20_01660 {ECO:0000313|EMBL:KQS51768.1};
OS Sphingomonas sp. Leaf198.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736299 {ECO:0000313|EMBL:KQS51768.1, ECO:0000313|Proteomes:UP000050871};
RN [1] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Garrido-Oter R.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Vorholt J.;
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 -!- 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:KQS51768.1}.
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DR EMBL; LMPX01000001; KQS51768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5USE1; -.
DR STRING; 1736299.ASG20_01660; -.
DR Proteomes; UP000050871; 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; 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: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; PS51318; TAT; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KQS51768.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050871}.
FT DOMAIN 710..779
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 790 AA; 83530 MW; 10EF53CF753DBAB5 CRC64;
MAPTRRDLLG LFGSVSVGGL IPGIAQAATA LPIYRDARAP VDFRVRDLMA RMTLEEKVGQ
TISLWATKAD VMTPGGLDFD PARASAAYPA GFGQVTRPSD KRGGPSVAAV AGGTGAQWRG
SASTIAFVNA VQRWARGTRL GIPVIFHEES LHGYMAPDAT MFPQAIGMAG SFDRDLMRRG
QAIIGREVRA HGSHLSLSPV VDIARDPRWG RIEETFGEDP YLCGEMGVAA VEGLQGDSTT
LAPGKVFATL KHMTGHGQPQ AGNNIGPAPI GERELRESFF PPFRAVVTRT GIGAVMPSYN
EIDGVPSHAN HWLLGEVLRG EWGFSGAIVS DYGAIEELDT IHHVARDLNG AAKLALAAGV
DSALPDGIAF RTLPAQVRAG TVPIAAVDAA CARMLALKFR AGLFEESAVD PRAAARLTGN
AEARGVALDA ARKSLCLLTN DGTLPLAPKG KIAVIGPNAA IARLGGYSSP PRQTVSLLDG
VRTFVGNAAT IVHAQGVFIT QSEDRSQDAV LLADPARNRA LIAEAVAVAR GADTIILAIG
DTEQTSREGF SKNHLGDRTT LDLIGEQNAL FDALHALGKP IVVAAINGRP PSWPNVMAKA
NAVLECWYPG QEGGTAMAEA LFGRINPGAK LPVTVVREVG QVPLYYNRKP STERGYLFAE
TAPLFPFGHG LSYTRFDISA PRLSAAKIGI AGSVGVEVDV ANIGQRAGDE VVQIYVRDQV
SSVARPVMEL KGFERVTLVP GERRTLRFTL GPDAFALWDV DMREVVEPGL FTIMAGPSSA
QVKTAVLEIA
//