| IED ID | IndEnz0009000017 |
| Enzyme Type ID | chitinase000017 |
| Protein Name |
Chitinase 2 EC 3.2.1.14 |
| Gene Name | CHT2 CAALFM_C504130CA CaO19.11376 CaO19.3895 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MLSFKSLLAAAVVASSALASASNQVALYWGQNGAGGQERLAQYCQEADVDIILLSFLNLFPDPLNVNFANQCGNTFESGLLHCSQIGADIKTCQSLGKTVLLSLGGGVGDYGFSDVASATKFADTLWNKFGAGEDPERPFDDAVVDGFDFDIEHGGATGYPELATALRGKFAKDTSKNYFLSAAPQCPYPDASLGDLLSKVPLDFAFIQFYNNYCSINGQFNYDTWSKFADSAPNKNIKLFVGVPATSNIAGYVDTSKLSSAIEEIKCDSHFAGVSLWDASGAWLNTDEKGENFVVQVKNVLNQNACVAPSSSATTQSTTTTSSAVTQSTTTTSAAITQSATTTSAAVATKSNQIVTSSSSSSSSIFYGNSTTESSTGIATGTVLPTGSNENAATTGSGSNTKLAISTVTDVQKTVITITSCSEHKCVATPVTTGVVVVTDIDTVYTTYCPLTNSQVYVSVKTVVCTEETCVPSPTSTSQKPKASTTIKGVEKGQTTSYPVVGTTEGVKKIVTTSAQTVGSSTKYVTIELTSTITPVTYPTSVASNGTNTTVPVFTFEGGAAVANSLNSVWFTVPFLLAAFAF |
| Enzyme Length | 583 |
| Uniprot Accession Number | P40953 |
| Absorption | |
| Active Site | ACT_SITE 153; /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: Chitinase involved in the remodeling of chitin in the fungal cell wall. Plays a role in cell separation. {ECO:0000269|PubMed:7708682}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (3); Lipidation (1); Propeptide (1); Sequence conflict (6); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cell wall;Chitin degradation;Chitin-binding;GPI-anchor;Glycoprotein;Glycosidase;Hydrolase;Lipoprotein;Membrane;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is positively regulated by BCR1 and FKH2. Transcription is greater during growth of the yeast form as compared to the mycelial form, and down-regulated by micafungin treatment. {ECO:0000269|PubMed:12455696, ECO:0000269|PubMed:16839200, ECO:0000269|PubMed:20859005, ECO:0000269|PubMed:7708682}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. |
| Modified Residue | |
| Post Translational Modification | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. {ECO:0000269|PubMed:21097664}.; PTM: Proteolytic cleavage by SAP9 and SAP10 leads to the cell wall release of CHT2 and increased chitinase activity, suggesting a direct influence of SAP9 and SAP10 on CHT2 function. {ECO:0000269|PubMed:21097664}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 60,815 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |