| 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; |