| IED ID | IndEnz0009000209 |
| Enzyme Type ID | chitinase000209 |
| Protein Name |
Basic 30 kDa endochitinase EC 3.2.1.14 |
| Gene Name | CHI9 |
| Organism | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Solanoideae Solaneae Solanum Solanum subgen. Lycopersicon Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
| Enzyme Sequence | MRLSEFTTLFLLFSVLLLSASAEQCGSQAGGALCASGLCCSKFGWCGNTNEYCGPGNCQSQCPGGPGPSGDLGGVISNSMFDQMLNHRNDNACQGKNNFYSYNAFVTAAGSFPGFGTTGDITARKREIAAFLAQTSHETTGGWPTAPDGPYAWGYCFLREQGSPGDYCTPSSQWPCAPGRKYFGRGPIQISHNYNYGPCGRAIGVDLLNNPDLVATDPVISFKSAIWFWMTPQSPKPSCHDVITGRWQPSGADQAANRVPGFGVITNIINGGLECGHGSDSRVQDRIGFYRRYCGILGVSPGENLDCGNQRSFGNGLLVDIM |
| Enzyme Length | 322 |
| Uniprot Accession Number | Q05538 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P29022 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Defense against chitin-containing fungal pathogens. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (7); Domain (1); Modified residue (2); Propeptide (1); Sequence conflict (5); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cell wall;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Hydroxylation;Plant defense;Polysaccharide degradation;Reference proteome;Secreted;Signal;Vacuole |
| Interact With | |
| Induction | INDUCTION: By fungal infection. |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:9188482}. Secreted, cell wall {ECO:0000269|PubMed:9188482}. Note=Vacuolar, protoplast and cell wall. |
| Modified Residue | MOD_RES 66; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 68; /note=4-hydroxyproline; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:9188482 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,345 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |