| IED ID | IndEnz0009000028 |
| Enzyme Type ID | chitinase000028 |
| Protein Name |
Endochitinase B EC 3.2.1.14 Chitinase B |
| Gene Name | chiB AN4871 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MSGYKTVGYFVNWAIYGRNYNPQDLPAEKLTHILYAFANVRPETGEVYLSDTWSDIEKHYPTDSWNDTGNNVYGCVKQLGLLKRQHRQLKVLLSIGGWTYSPNFTNGAGTPENRARFAQTATKLITDLGFDGIDIDWEYPQNDQQAQNYVDLLRRCREALNAAQGQRRFQLTVAVPAGPDNYNKLRLQEMTPYLDFYNLMAYDYAGSWDQTAGHQANLYPSTSNPTSTPFNTVQAVNHYIDAGGVPSNKIILGMPIYGRAFQNTDGPGRPYSGIGQGTWEQGVYDYKALPRPGATEQLDTNIGASWSYDPSSREMVSYDTVAAADLKAAYIQSRRLGGAMWWETSADKGGKTANKADGSLIGTFVEDVGGVNNLDRTQNAISYPDSQYDNLKAGFPSS |
| Enzyme Length | 398 |
| Uniprot Accession Number | G5EAZ3 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | |
| Binding Site | BINDING 139; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 342; /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:0000269|PubMed:18800599}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Major 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). Plays a role in the morphogenesis and autolysis. Has also significant antifungal activity against various fungal species. {ECO:0000269|PubMed:19486415, ECO:0000269|PubMed:23124755}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.5. {ECO:0000269|PubMed:18800599}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Domain (1); Glycosylation (2); Region (3) |
| Keywords | Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted |
| Interact With | |
| Induction | INDUCTION: Expression is increased at the beginning of the stationary phase of growth and reaches maximum in the early autolytic phase of growth. {ECO:0000269|PubMed:19486415}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25043916}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,206 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |