ID E1SHM5_PANVC Unreviewed; 737 AA.
AC E1SHM5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=bglX {ECO:0000313|EMBL:ADO08824.1};
GN OrderedLocusNames=Pvag_0622 {ECO:0000313|EMBL:ADO08824.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO08824.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO08824.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO08824.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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}.
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DR EMBL; CP002206; ADO08824.1; -; Genomic_DNA.
DR AlphaFoldDB; E1SHM5; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR KEGG; pva:Pvag_0622; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_6; -.
DR Proteomes; UP000006631; Chromosome.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
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}.
FT DOMAIN 657..726
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 737 AA; 80839 MW; 1209A9D45BB6A5CB CRC64;
MTEQARDAFV NQLLKKMTLD EKIGQLRLIS VGPDNPKEAI RDMIQKSQVG AIFNTVTRQD
IRAMQDQAMQ LSRLKIPLFF AFDVIHGQRT IFPIPLALAA SWDLDAVKEV GRVSAYEAAD
DGLNMTWAPM VDVSREPRWG RGSEGFGEDT YLTSEMGRSM VQAMQGKSAA DRYSVMTSVK
HFALYGAVEG GRDYNTVDMS PQRMFQDYLP PYKASLDAGS GGVMVALNSI NGVPATADSW
LLKDLLRDKW KFKGITISDH GAIKELIKHG VASDPQEAVR IALKSGVDMS MSDEYYSKYL
PDLVKSGDVT MAEIDDAARH VLNVKYDMGL FNDPYSHLGP KEGDPQDTNA ESRLHRAEAR
DVARKSIVLL KNRLETLPLK KSGTIALIGP LADSQRDIMG SWSAAGVAKQ SVSLLQGMRN
ATEGKATLLY EKGANVSDNK GIQDFLNFYE QAVSVDTRSA EQMIDDAVAK AKQADVVVAA
VGEAQGMAHE ASSRSDLVIP PSQQKLLAAL KATGKPLVIV LMNGRPLSIV NEDRMADAVL
ETWFSGTEGG NAIADVLFGD YNPSGKLPVS FPRSVGQIPI YYNHLPTGRP YNFAKPNKYT
SHYYDAVNGP LYPFGYGLSY TSFTVSPVKM SSPTMPRDGS VEASVTVTNS GKRDGATVVQ
MYLNDPVASI SRPVQELRGF KRIMLKAGES QTVTFKIDVD ALKFWNQQMQ HVAEPGKFNV
MIGLDSVRTE NAQFSYQ
//
