| IED ID | IndEnz0009000285 |
| Enzyme Type ID | chitinase000285 |
| Protein Name |
Endochitinase 3 EC 3.2.1.14 Chitinase 3 Fragment |
| Gene Name | chi3 CHIT30 |
| Organism | Metarhizium anisopliae (Entomophthora anisopliae) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Metarhizium Metarhizium anisopliae (Entomophthora anisopliae) |
| Enzyme Sequence | QAAPDEGRASGHKLTVYWGAEDDTTTLDDVCNDSSYDVVNLAFLSHFFSAGGYPKMSIGNLDGPSQAQKKAGATGLQDGSSLVKSIKNCQSKGKPVILSMGGATDYSDVQLNSDAQGQQIANTVWNLFLGGTDHKELRPFGDVKLDGVDLDNETNDGTGYLAMTKQFKANFQKDTSKKYYITAAPQCPYPDQSEPLDVCQLLDWVQVQFYNNGNCNIAQRGFAKAVKNWSKGIGSGVQLYIGALASGADGDEGYVHAATLNRAVNQVKAMNLPNFGGAMLWEAHSAVKNGQLPEED |
| Enzyme Length | 296 |
| Uniprot Accession Number | Q6QDR4 |
| 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; Evidence={ECO:0000269|PubMed:15808943, ECO:0000269|PubMed:23452951, ECO:0000269|Ref.1}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Participates in the infection process and directly acts in the penetration process of the host cuticle. Involved in heat-shock adaptation. {ECO:0000269|PubMed:15808943, ECO:0000269|PubMed:23452951, ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.0. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (3); Non-terminal residue (1) |
| Keywords | Carbohydrate metabolism;Chitin degradation;Chitin-binding;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Virulence |
| Interact With | |
| Induction | INDUCTION: Induced by chitin and cuticle and repressed by glucose. Protein expression is increased after host tick Boophilus microplus infection. Accumulates also in response to heat-shock stress conditions. {ECO:0000269|PubMed:15808943, ECO:0000269|PubMed:23452951}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,762 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.537 mM for p-nitrophenyl beta-N-diacetylchitobiose {ECO:0000269|Ref.1}; Vmax=4.86 nmol/min/mg enzyme toward p-nitrophenyl beta-N-diacetylchitobiose {ECO:0000269|Ref.1}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |