| IED ID | IndEnz0009000112 |
| Enzyme Type ID | chitinase000112 |
| Protein Name |
Endochitinase A EC 3.2.1.14 Chitinase A |
| Gene Name | chiA AN8241 |
| 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 | MAPKLFTFVSALSGLASLASAFHAEAKSNIAVYYGQGVNQPRLAEFCAETSYDIINIGFINSFPEQNPLTGLPGSDFGNQCWADTFVVDGIASQLYSHCPNIAEDIPKCQAAGKKVFLSLGGATPTYWFDTIDASTKLADFLWGAFGPVTDAWTVADKPRPFGNAVVDGFDFDIEFFGSKGYANMIKRFRRRFGEVPDQTFYISAAPQCSIPDEQLSVAIKNAVIDFVWVQFYNTPGCSARDFVLGTKNGFNYDSWVEVIKAGANPNAKLYVGLPASGAAANLGYYLTPEEVKPLVKKYMDKYPETFGGVMLWEATQARNNQIDGVGYNEKIREILYDLDPNHPPPTTSPTPTPTPSTTTTSTTSTTSTTSATSTTSTTSTTSTTSTTPTTSTTSTTSTTTPTPSPSPSTASSSTTETVTPSPKPSPSESSTTSETSSLPSTSTPVVSETPSETKTPTSSSAPPLSSSSPVGGSSSTASSSTSTPSETPSASSTRAVSETSTHISTSTSSGPETSLTGSSTSVPATSSSVPSSAISPSSTPVISETPRPPVTSSSSSTFVSSTSTSTDCSESSTAIGTHSSSSISETPSASTPAASPSTSPETTKTLTVFPTPGSSVSTGTTSASTLSSSVPATSGGHTETSTVSTSSANQTPSASTSKPLIPTNSASSTSTGSVTSTPSAPGVPSSSAGSDETATTSTTDSEPTSTSSGSVTAKPTTTEPATTTTIIVTSYTSICPTGFTTITTTITSTYCPGTASATATAIAPTTDVPGSGSGSSPAQPTITADIPEGWTTTVTVCTVCAATPTTVTLTLPPATTTEESTSAQPTGEVPSSDGSGSGEVSTTTVVVVPAPTGNAGDGVPAPGANVGEEYTAAPGSATTSKPLIGGGASGAHTAYPYASSTFHIIPSASAHVPVPSGSGSSPSGTQGGASPTFTGAGSRYDVVKGVPALVALALSLLAVL |
| Enzyme Length | 961 |
| Uniprot Accession Number | G5EB30 |
| 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; Evidence={ECO:0000269|PubMed:18420434}; |
| 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:18420434}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (2); Domain (1); Lipidation (1); Propeptide (1); Region (4); 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: Expressed specifically highly during conidia germination and in the marginal growth regions of colonies. {ECO:0000269|PubMed:18420434}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18420434}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18420434}. Secreted, cell wall {ECO:0000250}. Cell tip {ECO:0000269|PubMed:18420434}. Note=Localizes at the germ tubes of conidia, at hyphal branching sites and hyphal tips. |
| Modified Residue | |
| Post Translational Modification | PTM: O-glycosylated but not N-glycosylated. {ECO:0000269|PubMed:18420434}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 96,840 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |