| IED ID | IndEnz0004000029 |
| Enzyme Type ID | xylanase000029 |
| Protein Name |
Pectate lyase A EC 4.2.2.2 Pectin lyase EC 4.2.2.10 |
| Gene Name | pelA |
| Organism | Paenibacillus amylolyticus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus amylolyticus |
| Enzyme Sequence | MKKMLTLLLSAGLVASIFGVMPAAAAPTVVNSTIVVPKGTTYDGQGKTFVANPSTLGDGSQAENQKPVFRLEAGATLKNVIIGAPAADGVHCYGNCNISNVVWQDVGEDALTLKSSGTVNITGGAAYKAYDKVFQINAAGTINIKNFRADDIGKLVRQNGGTTFTVNMTLDNSNISNVKDAIMRTDSSSSQGRITNTRYSKVPTLFKGFASGKTSQSGNTQY |
| Enzyme Length | 222 |
| Uniprot Accession Number | D3JTC1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.2; Evidence={ECO:0000269|PubMed:20622125}; CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10; Evidence={ECO:0000269|PubMed:20622125}; |
| DNA Binding | |
| EC Number | 4.2.2.2; 4.2.2.10 |
| Enzyme Function | FUNCTION: Catalyzes the depolymerization of both polygalacturonate and pectins with low (20-34%) and high (90%) levels of methyl esterification, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Does not show xylanase and cellulase activity. {ECO:0000269|PubMed:20622125}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:20622125}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.5. {ECO:0000269|PubMed:20622125}; |
| Pathway | PATHWAY: Glycan metabolism; pectin degradation. {ECO:0000269|PubMed:20622125}. |
| nucleotide Binding | |
| Features | Chain (1); Signal peptide (1) |
| Keywords | Calcium;Carbohydrate metabolism;Lyase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,253 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 4.2.2.2; |