ID A0A0L7TIQ2_9GAMM Unreviewed; 765 AA.
AC A0A0L7TIQ2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=NG42_00710 {ECO:0000313|EMBL:KOC92862.1}, NG43_00460
GN {ECO:0000313|EMBL:KOC95219.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC95219.1, ECO:0000313|Proteomes:UP000036851};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC92862.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC95219.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC95219.1}.
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DR EMBL; JRXE01000001; KOC92862.1; -; Genomic_DNA.
DR EMBL; JRXF01000001; KOC95219.1; -; Genomic_DNA.
DR RefSeq; WP_052896718.1; NZ_JRXF01000001.1.
DR AlphaFoldDB; A0A0L7TIQ2; -.
DR STRING; 1560201.NG42_00710; -.
DR PATRIC; fig|1560201.3.peg.154; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; 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.
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:UP000037088};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..765
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010916900"
FT DOMAIN 685..754
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 765 AA; 83365 MW; 999F66434837FF07 CRC64;
MKWIYSVSLA VTLAMQPAFA DELSAPHPLT PQARDAFVSD LLKKMTLDEK IGQLRLITVG
PENTKEVIRG MIQQEQVGAI FNTVTRQDIR AMQDQAMQLS RLKIPLFFAY DVVHGQRTAF
PIPLGLAASW DLDALADVGR ISAYEAADDG LNMTWAPMVD VTREPRWGRV SEGFGEDTFL
TAEMGRTLVE SMQGNSAADR YSVMTSVKHY AAYGAVEGGR DYNTVDMSPQ RLLQDYLPPY
KAALDAGSGG VMVSLNSLNG VPATADSWLL KDILRDDWKF KGITISDHGA IKELIKHGVA
SDPEDAVRLA LKSGVNMSMN DEYYSKYLPG LVKRGVVSEQ EIDDATRHVL NVKYDMGLFN
DPYSHLGAKE SDPQDTNAES RLHRAEARDV ARKSMVLLKN RLETLPLKKS GTIALVGPLA
DSQNDIIGSW SAAAVSGQAV TLLQGIKNAT EGKATVLYAK GANVTDNKGI QDFLNLYENA
VNSDTRSAQQ MLDEAVVAAQ KADVVVAAVG EARGMAHEAS SRSDITIPPS QVKLLDALKA
TGKPLVIVLM NGRPLALVNE HQQADALLET WFSGTEGGNA IADVLFGDYN PSGKLPMSFP
RSVGQIPIYY NHLNTGRPYN FAKPNKYTSH YYDAANGPLF PFGYGLSYTT FTVSPVALSA
ASMPRDGKIN ASVTVTNTGK RDGATVVQMY LHDQVASISR PVKELKGFKR IMLKAGESQT
VTFPIDVDAL KFWNARMQQV AEPGKFSVMI GLDSAKTENA EFTYL
//
