| IED ID | IndEnz0009000004 |
| Enzyme Type ID | chitinase000004 |
| Protein Name |
Acidic endochitinase Pun g 14, amyloplastic EC 3.2.1.14 Chitinase III Pomegranate seed chitinase allergen Pun g 14 |
| Gene Name | PSC CDL15_Pgr011527 |
| Organism | Punica granatum (Pomegranate) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Myrtales Lythraceae Punica Punica granatum (Pomegranate) |
| Enzyme Sequence | MAKTLPFSRALLLSLSILLVARAISAGDIAIYWGQNGGEGTLASTCDTGRYAYVIVSFVTTFGNFRAPVVNLAGHCDPAAGTCTGLSDEIRSCQGKDIKVLMSIGGGAGDYSLVSEADADNFADYLWNNFLGGQSSSRPLGDAVLDGIDFDIELGTTTFYDTLARALSSRSTQAAKVYLTAAPQCPHPDSHLDAALNTGLFDNVWIQFYNNPLAQCQYSSGNTNDILSSWNTWTSSTTAGKIFLGLPAAPEAAGSGYIPPDVLTGQILPQIKTSAKYGGVMLYSKFYDTTYSTTIKDQV |
| Enzyme Length | 299 |
| Uniprot Accession Number | G1UH28 |
| Absorption | |
| Active Site | ACT_SITE 153; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01258, ECO:0000305|PubMed:25252615" |
| Activity Regulation | ACTIVITY REGULATION: Activity is not affected by addition of 10 mM Ca(2+) or removal of Ca(2+). {ECO:0000269|PubMed:21790816}. |
| 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:21790816}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Hydrolyzes chitin. Probable calcium storage protein of the seeds. Binds calcium ions with high capacity and low affinity. Involved in seed germination. {ECO:0000269|PubMed:21790816}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 45 degrees Celsius. Removal of Ca(2+) from the protein by EDTA treatment decreases the optimum temperature to 35 degrees Celsius. {ECO:0000269|PubMed:21790816}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 2.5 and 5.0. Removal of Ca(2+) from the protein by EDTA treatment narrows the pH range to 2.5-3.5. {ECO:0000269|PubMed:21790816}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Chain (1); Disulfide bond (3); Domain (1); Helix (14); Sequence conflict (2); Transit peptide (1); Turn (3) |
| Keywords | 3D-structure;Allergen;Amyloplast;Calcium;Carbohydrate metabolism;Chitin degradation;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Plastid;Polysaccharide degradation;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, amyloplast {ECO:0000269|PubMed:21790816, ECO:0000269|PubMed:22112454}. Note=Localizes to stroma in amyloplasts of the embryonic cells of the seed. {ECO:0000269|PubMed:21790816, ECO:0000269|PubMed:22112454}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4TOQ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,747 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat/KM is 0.119 M(-1)sec(-1) for native protein, 0.130 M(-1)sec(-1) for native protein with 10 mM Ca(2+) and 0.116 M(-1)sec(-1) for EDTA-treated protein, using 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (4-MU(GlcNAc)(3)) as substrate at pH 4.5 and 37 degrees Celsius. {ECO:0000269|PubMed:21790816}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |