| IED ID | IndEnz0009000002 |
| Enzyme Type ID | chitinase000002 |
| Protein Name |
Endochitinase 4 EC 3.2.1.14 Chitinase class IV CJP-4 allergen Cry j Chitinase |
| Gene Name | |
| Organism | Cryptomeria japonica (Japanese cedar) (Cupressus japonica) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Acrogymnospermae Pinopsida Pinidae Conifers II Cupressales Cupressaceae Cryptomeria Cryptomeria japonica (Japanese cedar) (Cupressus japonica) |
| Enzyme Sequence | MQIMATQNSKSNIFWSSSASVVLVLLLLVDVGVCQNCGCNGLCCSQYGYCGSGEAYCGAGCKEGPCSSSSPPSTGTGVGSIVSSDVFNSIVGGAASGCAGNGFYTYDSFISAANAFNGFGTSGSSDVNKREIAAFFANAAHETGGFCYIEEQNPTSIYCDASNTQYPCASGKTYHGRGPLQLSWNYNYGAAGSYIQFDGLNNPEIVGTDSTISFKTAVWFWMVNSNCHTAITSGQGFGATIRAINSMECDGGNAATVASRVNYYQKFCQQLNVDTGSNLQC |
| Enzyme Length | 281 |
| Uniprot Accession Number | Q5NTA4 |
| Absorption | |
| Active Site | ACT_SITE 142; /note="Proton donor"; /evidence="ECO:0000255|PIRSR:PIRSR001060-1, ECO:0000269|PubMed:28032262" |
| 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; Evidence={ECO:0000269|PubMed:15725197, ECO:0000269|PubMed:29756783}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Has endochitinase activity (PubMed:15725197). Hydrolyzes chitin oligosaccharides, GlcNAc(n), with different degrees of polymerization (n=2-6), a soluble substrate glycol chitin, and an insoluble substrate beta-chitin nanofiber in vitro. GlcNAc(6) is hydrolyzed at the second glycosidic linkage from the reducing end in addition to the middle linkage. GlcNAc(4) is further hydrolyzed to GlcNAc(2). Has antifungal activity against hyphal growth of H.rufa (PubMed:29756783). {ECO:0000269|PubMed:15725197, ECO:0000269|PubMed:29756783}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (2); Chain (1); Disulfide bond (7); Domain (1); Helix (12); Mutagenesis (2); Sequence conflict (3); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Allergen;Antimicrobial;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Fungicide;Glycosidase;Hydrolase;Plant defense;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P29022}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:15725197}. |
| Signal Peptide | SIGNAL 1..34; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5H7T; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,355 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |