Detail Information for IndEnz0002018445
IED ID IndEnz0002018445
Enzyme Type ID protease018445
Protein Name Beta-glucosidase 23
AtBGLU23
EC 3.2.1.21
Protein PHOSPHATE STARVATION-RESPONSE 3.1
Gene Name BGLU23 PSR3.1 PYK10 At3g09260 F3L24.13
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MVLQKLPLIGLLLLLTIVASPANADGPVCPPSNKLSRASFPEGFLFGTATAAYQVEGAINETCRGPALWDIYCRRYPERCNNDNGDVAVDFFHRYKEDIQLMKNLNTDAFRMSIAWPRIFPHGRKEKGVSQAGVQFYHDLIDELIKNGITPFVTVFHWDTPQDLEDEYGGFLSERIVKDFREYADFVFQEYGGKVKHWITFNEPWVFSHAGYDVGKKAPGRCSSYVNAKCQDGRSGYEAYLVTHNLLISHAEAVEAYRKCEKCKGGKIGIAHSPAWFEAHDLADSQDGASIDRALDFILGWHLDTTTFGDYPQIMKDIVGHRLPKFTTEQKAKLKASTDFVGLNYYTSVFSNHLEKPDPSKPRWMQDSLITWESKNAQNYAIGSKPLTAALNVYSRGFRSLLKYIKDKYANPEIMIMENGYGEELGASDSVAVGTADHNRKYYLQRHLLSMQEAVCIDKVNVTGYFVWSLLDNFEWQDGYKNRFGLYYVDFKNNLTRYEKESGKYYKDFLSQGVRPSALKKDEL
Enzyme Length 524
Uniprot Accession Number Q9SR37
Absorption
Active Site ACT_SITE 203; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 418; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Activated by tissue damage and upon binding to PBP1 or PBP2. {ECO:0000269|PubMed:15919674, ECO:0000269|PubMed:19965874}.
Binding Site BINDING 54; /note=Substrate; /evidence=ECO:0000250; BINDING 157; /note=Substrate; /evidence=ECO:0000250; BINDING 202; /note=Substrate; /evidence=ECO:0000250; BINDING 346; /note=Substrate; /evidence=ECO:0000250; BINDING 468; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:19965874};
DNA Binding
EC Number 3.2.1.21
Enzyme Function FUNCTION: Beta-D-glucosidase active on scopolin > esculin >> 4-MU-glucoside >> DIMBOA-glucoside. No activity with pNP-glucoside, oNP-glucoside and sinigrin as substrates. May possess beta-D-fucosidase activity. Required for the beneficial interaction with the endophytic fungus P.indica. May participate in the control of root colonization by P.indica by repressing defense responses and modulating other responses required for a mutualistic interaction. {ECO:0000269|PubMed:15155889, ECO:0000269|PubMed:15919674, ECO:0000269|PubMed:18248598, ECO:0000269|PubMed:19965874}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:19965874};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:19965874};
Pathway
nucleotide Binding
Features Active site (2); Binding site (5); Chain (1); Disulfide bond (1); Erroneous initiation (1); Frameshift (1); Glycosylation (3); Motif (1); Mutagenesis (1); Region (1); Sequence conflict (5); Signal peptide (1)
Keywords Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Signal
Interact With
Induction INDUCTION: Up-regulated by wounding, 2,4-D and methyl jasmonate (MeJA). Down-regulated by salt and mannitol. {ECO:0000269|PubMed:15919674, ECO:0000269|PubMed:19965874}.
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12581307, ECO:0000269|PubMed:15155889, ECO:0000269|PubMed:15919674, ECO:0000269|PubMed:18248598, ECO:0000269|PubMed:19147648}. Note=Located in ER bodies.
Modified Residue
Post Translational Modification PTM: Forms interchain disulfide bonds.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000269|PubMed:12581307
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12881493; 14551330; 14617066; 15539469; 16526091; 17376161; 17432890; 17916636; 18324730; 18780803; 19847124; 21205622; 21355997; 22102697; 22611176; 23166355; 24064926; 25282558; 26479492; 27612205; 29106622; 30696747; 30770459; 31132914; 33315514; 7640358; 9177312;
Motif MOTIF 521..524; /note=Prevents secretion from ER; /evidence=ECO:0000255|PROSITE-ProRule:PRU10138
Gene Encoded By
Mass 59,721
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.81 mM for scopolin (with recombinant enzyme) {ECO:0000269|PubMed:19965874}; KM=0.73 mM for scopolin (with native enzyme) {ECO:0000269|PubMed:19965874}; KM=9.7 mM for esculin (with recombinant enzyme) {ECO:0000269|PubMed:19965874}; KM=5.8 mM for esculin (with native enzyme) {ECO:0000269|PubMed:19965874};
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.21;