| IED ID | IndEnz0011000011 |
| Enzyme Type ID | glucanase000011 |
| Protein Name |
Exo-beta-1,3-glucanase EC 3.2.1.58 Glucan 1,3-beta-glucosidase Laminarinase SacteLam55A |
| Gene Name | SACTE_4363 |
| Organism | Streptomyces sp. (strain SirexAA-E / ActE) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces unclassified Streptomyces Streptomyces sp. (strain SirexAA-E / ActE) |
| Enzyme Sequence | MHVPPTDPARSAPPASPHRRRRPKALGLTALAAAMLMAVPTTQAAFGSDVRPAAAQEVVGGGDLGPNVLVFDPSTPDIQGKVDEVFRKQESNQFGTDRYALMFKPGTYNDINAQIGFYTSIAGLGLNPDDTTFNGDVTVDAGWFDGNATQNFWRSAENLALNPVNGTNRWAVSQAAPFRRMHVKGGLNLAPDGYGWASGGYIADSKIDGEVGPYSQQQWYTRDSSVGGWGNGVWNMTFSGVEGAPAQSFPEPPYTTLETTPVSREKPFLYLDGDDYKVFVPAKRTNARGTSWGNGTPEGESLPLDQFYVVKPGATAETINAAVDQGLHLLFTPGVYHVDQPIEIDRANTVALGLGLATIIPDNGVTALKVGDVDGVKVAGLLVDAGPVNSETLVEVGSDGASGDHAANPTSLQDVFVRIGGAGPGKATTSIVVNSNDTIIDHTWVWRADHGEGVGWETNRADYGVHVKGDNVLATGLFVEHFNKYDVQWSGENGKTIFYQNEKAYDAPDQAAIQNGDIKGYAAYKVDDSVTTHEGWGMGSYCYFNVNPDIRQQHGFQAPVKPGVKFHDLLVVSLGGKGQYEHVINDIGDPTSGDTTIPSQVVSFP |
| Enzyme Length | 605 |
| Uniprot Accession Number | G2NFJ9 |
| Absorption | |
| Active Site | ACT_SITE 502; /note=Proton donor; /evidence=ECO:0000305|PubMed:25752603 |
| Activity Regulation | |
| Binding Site | BINDING 174; /note=Substrate; /evidence=ECO:0000269|PubMed:25752603; BINDING 217; /note=Substrate; /evidence=ECO:0000269|PubMed:25752603; BINDING 505; /note=Substrate; /evidence=ECO:0000269|PubMed:25752603 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; Evidence={ECO:0000269|PubMed:25752603}; |
| DNA Binding | |
| EC Number | 3.2.1.58 |
| Enzyme Function | FUNCTION: Exo-beta-1,3-glucanase that specifically hydrolyzes laminarin and laminarioligosaccharides, producing glucose and laminaribiose as end products. {ECO:0000269|PubMed:25752603}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Maintains 70% or more of the maximal activity from 35 to 65 degrees Celsius. {ECO:0000269|PubMed:25752603}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Maintains 70% or more of the maximal activity from pH 6.0 to 9.0. {ECO:0000269|PubMed:25752603}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (48); Binding site (3); Chain (1); Helix (7); Mutagenesis (8); Region (4); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Is up-regulated during growth on biomass, i.e. when the bacterium is grown on cellobiose, xylan, and various pretreated switchgrass samples. {ECO:0000269|PubMed:23301151}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23301151}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..44; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 4PEW; 4PEX; 4PEY; 4PEZ; 4PF0; 4TYV; 4TZ1; 4TZ3; 4TZ5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,661 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.93 mg/ml for L.digitata soluble laminarin (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:25752603}; Vmax=128 umol/min/mg enzyme with L.digitata soluble laminarin as substrate (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:25752603}; Note=kcat is 138 sec(-1) with L.digitata soluble laminarin as substrate (at pH 6 and 40 degrees Celsius). {ECO:0000269|PubMed:25752603}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |