| IED ID | IndEnz0009000009 |
| Enzyme Type ID | chitinase000009 |
| Protein Name |
Basic endochitinase C EC 3.2.1.14 Rye seed chitinase-c RSC-c |
| Gene Name | rscc |
| Organism | Secale cereale (Rye) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Secale Secale cereale (Rye) |
| Enzyme Sequence | MRSLAVVVAVVATVAMAIGTAHGSVSSIISHAQFDRMLLHRNDGACQAKGFYTYDAFVAAANAFPGFGATGSTDARKRDVAAFLAQTSHETTGGWATAPDGAFAWGYCFKQERGAAADYCTPSAQWPCAPGKRYYGRGPIQLSHNYNYGPAGRAIGVDLLRNPDLVATDPTVSFKTALWFWMTAQAPKPSSHAVITGKWSPSGADRAAGRAPGFGVITNIINGGLECGHGQDSRVADRIGFYKRYCDILGVGYGDNLDCYNQRPFA |
| Enzyme Length | 266 |
| Uniprot Accession Number | Q9FRV0 |
| Absorption | |
| Active Site | ACT_SITE 90; /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; Evidence={ECO:0000269|PubMed:11999399, ECO:0000269|PubMed:7763659}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Defense against chitin-containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin. {ECO:0000269|PubMed:11826968, ECO:0000269|PubMed:11999399, ECO:0000269|PubMed:12092848}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Enzyme activity is retained almost fully under 40 degrees Celsius and completely destroyed at 70 degrees Celsius. At 60 degrees Celsius the activity was 15-30% compared to the untreated enzyme. {ECO:0000269|PubMed:7763659}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 5.0. Stable between pH 4-8. {ECO:0000269|PubMed:7763659}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (4); Chain (1); Disulfide bond (3); Helix (12); Mutagenesis (5); Signal peptide (1); Site (2); Turn (5) |
| Keywords | 3D-structure;Antimicrobial;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Fungicide;Glycosidase;Hydrolase;Plant defense;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence="ECO:0000269|PubMed:11999399, ECO:0000269|PubMed:7763659, ECO:0000269|PubMed:7764335" |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 4DWX; 4DYG; 4J0L; |
| Mapped Pubmed ID | 22831795; 23871710; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,302 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |