| IED ID | IndEnz0009000054 |
| Enzyme Type ID | chitinase000054 |
| Protein Name |
Endochitinase A EC 3.2.1.14 Chitinase A |
| Gene Name | chiA |
| Organism | Emericella nidulans (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) |
| Enzyme Sequence | MAPKLFTFVSALSGLASLASAFHAEAKSNIAVYYGQGVNQPRLAEFCAETSYDIINIGFINSFPEQNPLTGLPGSDFGNQCWADTFVVDGIASQLYSHCPNIAEDIPKCQAAGKKVFLSLGGATPTYWFDTIDASTKLADFLWGAFGPVTDAWTVADKPRPFGNAVVDGFDFDIEFFGSKGYANMIKRFRRRFGEVPDQTFYISAAPQCSIPDEQLSVAIKNAVIDFVWVQFYNTPGCSARDFVLGTKNGFNYDSWVEVIKAGANPNAKLYVGLPASGAAANLGYYLTPEEVKPLVKKYMDKYPETFGGVMLWEATQARNNQIDGVGYNEKIREILYDLDPNHPPPTTSPTPTPTPSTTTTSTTSTTSTTSATSTTSTTSTTSTTSTTPTTSTTSTTSTTTPTPSPSPSTASSSTTETVTPSPKPSPSESSTTSETSSLPSTSTPVVSETPSETKTPTSSSAPPLSSSSPVGGSSSTASSSTSTPSETPSASSTRAVSETSTHISTSTSSGPETSLTGSSTSVPATSSSVPSSAISPSSTPVISETPRPPVTSSSSSTFVSSTSTSTDCSESSTAIGTHSSSSISETPSASTPAASPSTSPETTKTLTVFPTPGSSVSTGTTSASTLSSSVPATSGGHTETSTVSTSSANQTPSASTSKPLIPTNSASSTSTGSVTSTPSAPGVPSSSAGSDETATTSTTDSEPTSTSSGSVTAKPTTTEPATTTTIIVTSYTSICPTGFTTITTTITSTYCPGTASATATAIAPTTDVPGSGSGSSPAQPTITADIPEGWTTTVTVCTVCAATPTTVTLTLPPATTTEESTSAQPTGEVPSSDGSGSGEVSTTTVVVVPAPTGNAGDGVPAPGANVGEEYTAAPGSATTSKPLIGGGASGAHTAYPYASSTFHIIPSASAHVPVPSGSGSSPSGTQGGASPTFTGAGSRYDVVKGVPALVALALSLLAVL |
| Enzyme Length | 961 |
| Uniprot Accession Number | Q92223 |
| 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 (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;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is induced during conidiospore formation (PubMed:9501518). Significantly up-regulated expression with colloidal chitin and chito-oligomers, namely N-acetyl-D-glucosamine (GlcNAc), N,N'-diacetylchitobiose (GlcNAc)2 and N,N',N''-triacetylchitotriose (GlcNAc)3. Expression is not affected by changes in the levels of reactive oxygen species or in the glutathione-glutathione disulfide redox balance, the changes which are physiological characteristics developing in aging and autolyzing fungal cultures. Down-regulated by the oxidative-stress-generating agent diamide, but not by menadione or hydrogen peroxide (PubMed:17455791). {ECO:0000269|PubMed:17455791, ECO:0000269|PubMed:9501518}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Cell tip {ECO:0000250}. Note=Localizes at the germ tubes of conidia, at hyphal branching sites and hyphal tips. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: O-glycosylated but not N-glycosylated. {ECO:0000250}. |
| 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 | 3.2.1.14; |