| IED ID | IndEnz0009000099 |
| Enzyme Type ID | chitinase000099 |
| Protein Name |
Endochitinase A1 EC 3.2.1.14 Chitinase A1 |
| Gene Name | chiA1 chi1 |
| Organism | Neosartorya fumigata (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) |
| Enzyme Sequence | MVSSKLSFVATAVAALAPLASAFDASSRSNLAIYWGQGPNQLRLSHFCQETSLDIINIGFINYFPDMSPGHWPGSNFGNQCDGSVYVTNDGVVTKLLSGCHQIMEDIPICQAAGKKVLLSIGGAYPPDQSILSEDSAVAFATFLWGAFGPVAEGWEGPRPFGDVVVDGFDFDIEHNGGFGYATMVNTFRQYFNQVPERKFYLSAAPQCIIPDAQLSDAIFNAAFDFIWIQYYNTAACSAKSFIDTSLGTFNFDAWVTVLKASASKDAKLYVGLPASETAANQGYYLTPDEVESLVSTYMDRYPDTFGGIMLWEATASENNQIDGAPYADHMKDILLHCDPSPPVTSSSAVPSSTPVTTPSPSSSAVPSSTPAVSETPSPSSSAVPSSTPVASSTPVVPGTSASSSPVSSSSAIAPSTPVVPGTSTPSSTPVASSTPVVPGTSASSSPVSSSSAVASSTPVVPGTSVPSSTPAIPGGSSSSSEAVASSTPLVTLTLTVSPTPAPSSSESSSTDLSSSTQTDVGTAPSQPAGPSTTATATTSSSSSSTDESSTTVGSGNGNGSGSTTTTAATDSITAAPTATSSATATGATSEPVTITTIIVTSYIDICPTGFTTVTTTYTTTYCPGTNTATATATVTNPPSGPGGAGSQTTAPTVPEGWTTTVTVCTQCAAKPTTVTLTLPVTETGSTSTDAVPAPPAATGEGSNPTQPSGASPTGGNGSFSEEPVPPPAVTQVSTSTEIVTLVRPTSSRPLILGTGTVHPSSTLAVKPSAKPSGQNSGSSSHVPIPPSYTQEAVSPLSTGAASRVTGLGHGLVLTVLTLSAFFVL |
| Enzyme Length | 825 |
| Uniprot Accession Number | Q873Y0 |
| Absorption | |
| Active Site | ACT_SITE 174; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | ACTIVITY REGULATION: The cyclic peptide natural product argifin acts as a specific inhibitor. {ECO:0000269|PubMed:21168763}. |
| 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:16096835, ECO:0000269|PubMed:21168763}; |
| 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. {ECO:0000269|PubMed:21168763}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Compositional bias (2); Domain (1); Glycosylation (2); Helix (15); Lipidation (1); Propeptide (1); Region (5); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cell membrane;Cell wall;Chitin degradation;Chitin-binding;GPI-anchor;Glycoprotein;Glycosidase;Hydrolase;Lipoprotein;Membrane;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Shows high levels of constitutive expression and repressed by caspofungin. {ECO:0000269|PubMed:16096835, ECO:0000269|PubMed:20974863}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted, cell wall {ECO:0000269|PubMed:16096835, ECO:0000269|PubMed:20974863}. |
| Modified Residue | |
| Post Translational Modification | PTM: O-mannosylated by pmt4. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2XUC; 2XVN; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 83,088 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for 4-methylumbelliferyl beta-D-N,N'-diacetylchitobiose {ECO:0000269|PubMed:21168763}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |