| IED ID | IndEnz0009000116 |
| Enzyme Type ID | chitinase000116 |
| Protein Name |
Hevamine-A Includes: Chitinase EC 3.2.1.14 ; Lysozyme EC 3.2.1.17 |
| Gene Name | |
| Organism | Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Malpighiales Euphorbiaceae Crotonoideae Micrandreae Hevea Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) |
| Enzyme Sequence | MAKRTQAILLLLLAISLIMSSSHVDGGGIAIYWGQNGNEGTLTQTCSTRKYSYVNIAFLNKFGNGQTPQINLAGHCNPAAGGCTIVSNGIRSCQIQGIKVMLSLGGGIGSYTLASQADAKNVADYLWNNFLGGKSSSRPLGDAVLDGIDFDIEHGSTLYWDDLARYLSAYSKQGKKVYLTAAPQCPFPDRYLGTALNTGLFDYVWVQFYNNPPCQYSSGNINNIINSWNRWTTSINAGKIFLGLPAAPEAAGSGYVPPDVLISRILPEIKKSPKYGGVMLWSKFYDDKNGYSSSILDSVLFLHSEECMTVL |
| Enzyme Length | 311 |
| Uniprot Accession Number | P23472 |
| Absorption | |
| Active Site | ACT_SITE 153; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; |
| DNA Binding | |
| EC Number | 3.2.1.14; 3.2.1.17 |
| Enzyme Function | FUNCTION: Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Chain (1); Disulfide bond (3); Domain (1); Helix (17); Natural variant (2); Propeptide (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Carbohydrate metabolism;Chitin degradation;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Signal;Vacuole |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole. Note=In the lutoids (vacuoles) from rubber latex. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:1879417 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1HVQ; 1KQY; 1KQZ; 1KR0; 1KR1; 1LLO; 2HVM; |
| Mapped Pubmed ID | 11846790; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,718 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |