ID B8L1I7_9GAMM Unreviewed; 724 AA.
AC B8L1I7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SSKA14_2713 {ECO:0000313|EMBL:EED39696.1};
OS Stenotrophomonas sp. SKA14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=391601 {ECO:0000313|EMBL:EED39696.1};
RN [1] {ECO:0000313|EMBL:EED39696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA14 {ECO:0000313|EMBL:EED39696.1};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (DEC-2008) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS999412; EED39696.1; -; Genomic_DNA.
DR RefSeq; WP_008267094.1; NZ_DS999412.1.
DR AlphaFoldDB; B8L1I7; -.
DR HOGENOM; CLU_004542_5_1_6; -.
DR Proteomes; UP000003991; 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: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; PS50890; PUA; 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 642..711
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 724 AA; 78099 MW; D537661DF65CC06A CRC64;
MASDRIESLI AQMTVEEKVG QLGVFADMVR PFAPDVNPEA NVRNADQVLQ QVREGKVGSL
FNGVGAELGR RIQQVATEES RLGIPVILAA DVIHGMRTVF PIPLGEAASF EPELAERTAR
ATAIEATAAG LHWTYAPAVD IARDQRWGRG AEGAGEDVVL GCAFAAARVR GFQGSDLRAD
DSLLATPKHF AAYGAVMAGM EYNMVDISPQ TLRDVHLPPF KAAFDAGAIT VMSSFNDING
VPASANAELL TDILRGEWKF PGVVISDYTA DMELVAHGYA ADDRDATAKA FTAGLDLSMQ
SGFYAEHLPG LVESGDVPMA VLDEGVRRIL WLKEAIGLFD DPYRSLDPAR EADTSHIAAH
DELSRDAARR SIVLLNNRDN VLPLQKNGQK IALIGPFVQD RENIEGCWTL FGDKQRYVDL
ETGVRAAIGD EALLEIVPGC ELETAIAGGT EAAVAAALRA DVVVLALGEP QRYSGEAQSR
VEITLPPAQQ ALAEAVAMTG KPLVVLLRNG RALALQGAVR NAQAVAVTWY LGTQTGHAVA
DVLFGDYSPS ARLPVSFPQV SGQQPYFYNH PRTGRPELPT MSEFKARWRE IPNEPLYPFG
HGIGYTSFDY GVPQLSAAQL GWDETLTLTT TLTNSGEVAG EEVVQLYIHD RVASRVRPVR
ELKDFRKVAL QPGESAEVVF TLTREQLAFT GRDGVLRAEP GQFDVWVCAS SAAGEAVQFE
LLKG
//
