| IED ID | IndEnz0009000251 |
| Enzyme Type ID | chitinase000251 |
| Protein Name |
Endochitinase A EC 3.2.1.14 Chitinase A |
| Gene Name | ctcA chiF cts1 An09g06400 |
| Organism | Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
| Enzyme Sequence | MVFKPLTIAAAIAGLTPFVSAFDAQAKSNVAVYYGQGYGQQRLSHFCQETSLDIINIGFINTFPDQGAAGWPGSNFGNQCDGLTYEVDGVSTKLLSGCHQIAEDIPICQAAGKKVLLSLGGASPDNQQILSDASAVRFADFLWGAFGPQTEEWVSNDGPRPFGEVVVDGFDFDIEHNGGFGYATMVNRFRELFALVPERTFYISGAPQCPIPDPQLSDAIAQSPFDFVWVQFYNTAGCAASDSINGVSTGFNFDDWVDVIKRGANPDAKLYVGLPAGPGAAGAGYYLTPEEVYPLVDVYMNLYPETFGGIMLWEATASDENTFSGLTFADVIKDILVAVDPSPPVPSPSSSSVIASSTPVASSTPVASSAPASSTPISSGSPVPSSSAVSSSPAVSSTTESSSTQVVSGSVSASSSPITSSPVASSTPVASSAPSATSSAVASSSPIAPSSPVASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSAIASSSPVAPSSPVASSSPAVSSSAIVSSTPAVSTPVASSIPVISSPAIASGSAIASSSHVASSSTPAASSSPAVSSSPVASSSPALSSSPSASASSTPIIPSSTASSAVVSSSPTPSSSVVRSSSLLSSSSPALSSTRTPSNPVIPSSSAISITPSSTPVRSTSSVAPGKSSSAPVIPKPSSTVIATFTSSSGSLPSSSAPAGSGVPSSSTLPHPSSTSLLSSSPVSSAEPVSSSSAVGTSVGSSSNVVTGVSTRSSSSVVPSGTPIPPVSGTATESVTSSSSGSGSPTVPSSINTSSTDASSSSSASSVEPTSSGSVITSVTSSSASRVSSSSSSVVITNPSVPSDSSSSSGSELSTTSSTESTSSASSQTGAPTTSVSLGSSEAASTSTSGAAASGSGAQDSTKPTDHASTLSPSYSTPLASASGQTGSPTTVPAGIPTGNGSGLAPITSSITSAQAVPSVTSSGLESEPEPTITTTVIVTSYIDICPEGFTTITTTYTTTYCPATVSATATATAAVTNPPGAPAQTTSPSVPEGWTTTVTVCTHCAPTPTTVTLTLPATNRPSALASSTSAPNSPEDWTTTVSVCTDCGPTPTTVTVTIPVGAATGVDALTASPSGSQPAGESSPGQSAPTAPASTAPTTTETVIVVPSQSSTSQPVILGTGSVRASSTFHIQPSQSGSRVPVAPSGTAAGVSPVFTGAASRVSRLQHGAGAVSAFALFLLAAI |
| Enzyme Length | 1257 |
| Uniprot Accession Number | A2QUQ2 |
| Absorption | |
| Active Site | ACT_SITE 175; /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; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: GPI-anchored 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). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Domain (1); Glycosylation (2); Lipidation (1); Propeptide (1); Region (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cell membrane;Cell wall;Chitin degradation;Chitin-binding;GPI-anchor;Glycoprotein;Glycosidase;Hydrolase;Lipoprotein;Membrane;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Highly expressed in germinated conidia. Expression is induced by tunicamycin and DTT. {ECO:0000269|PubMed:17561995, ECO:0000269|PubMed:23449598}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: O-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 122,094 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |