| IED ID | IndEnz0009000189 |
| Enzyme Type ID | chitinase000189 |
| Protein Name |
Chitinase 2 EC 3.2.1.14 |
| Gene Name | chi2 |
| Organism | Yersinia entomophaga |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Yersiniaceae Yersinia Yersinia entomophaga |
| Enzyme Sequence | MVNKYTYTSSKAMSDISDVIGEPLAAWDSQVGGRVFNVIFDGKVYTNTYWVERWQVPGIGSSDGNPHNAWKFVRAATADEINKIGNPTTADVKPTENIPSPILVEDKYTEETYSRPDVNFKEDGSQGNLSYTATRVCAPMYNHYVGDKTKPKLSAYITDWCQYDARLDGGGSKEEERGRGFDLATLMQNPATYDRLIFSFLGICGDIGNKSKKVQEVWDGWNAQAPSLGLPQIGKGHIVPLDPYGDLGTARNVGLPPESADTSIESGTFLPYYQQNRAAGLLGGLRELQKKAHAMGHKLDLAFSIGGWSLSSYFSALAENPDERRVFVASVVDFFVRFPMFSCVDIDWEYPGGGGDEGNISSDKDGENYVLLIKELRSALDSRFGYSNRKEISIACSGVKAKLKKSNIDQLVANGLDNIYLMSYDFFGTIWADYIGHHTNLYSPKDPGEQELFDLSAEAAIDYLHNELGIPMEKIHLGYANYGRSAVGGDLTTRQYTKNGPALGTMENGAPEFFDIVKNYMDAEHSLSMGKNGFVLMTDTNADADFLFSEAKGHFISLDTPRTVKQKGEYAAKNKLGGVFSWSGDQDCGLLANAAREGLGYVADSNQETIDMGPLYNPGKEIYLKSISEIKSK |
| Enzyme Length | 633 |
| Uniprot Accession Number | B6A879 |
| Absorption | |
| Active Site | ACT_SITE 349; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | ACTIVITY REGULATION: Toxin complex is secreted when grown at 25 degrees Celsius or less; at higher temperatures the proteins are present intracellularly but not secreted. {ECO:0000269|PubMed:21278295}. |
| Binding Site | BINDING 350; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 582; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| 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:0000305|PubMed:22108167}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295). The TC has an endochitinase activity (PubMed:21278295, PubMed:22158901) (Probable). This subunit might aid infection by degradation of the larval peritrophic membrane (Probable). {ECO:0000269|PubMed:21278295, ECO:0000269|PubMed:22158901, ECO:0000305|PubMed:22108167}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0, in the intact toxin complex optimum pH is pH 4.0 to pH 8.0. {ECO:0000269|PubMed:22108167}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (18); Binding site (2); Chain (1); Domain (1); Helix (26); Region (3); Turn (8) |
| Keywords | 3D-structure;Carbohydrate metabolism;Chitin degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21278295}. Note=Secreted when grown at 25 degrees Celsius or less, but not when grown at 30 or 37 degrees Celsius. {ECO:0000269|PubMed:21278295}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1); Electron microscopy (1) |
| Cross Reference PDB | 4DWS; 6OGD; |
| Mapped Pubmed ID | 31028251; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,668 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=230 uM for 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside {ECO:0000269|PubMed:22108167}; Note=In the intact toxin complex the combined chitinase activity of Chi1 and Chi2 is slightly reduced. {ECO:0000269|PubMed:22108167}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |