| IED ID | IndEnz0010001103 |
| Enzyme Type ID | esterase001103 |
| Protein Name |
Cutinase 1 EC 3.1.1.74 Cutin hydrolase 1 Fragment |
| Gene Name | |
| Organism | Colletotrichum kahawae (Coffee berry disease fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Glomerellales Glomerellaceae Colletotrichum Colletotrichum gloeosporioides species complex Colletotrichum kahawae (Coffee berry disease fungus) |
| Enzyme Sequence | VIYIFAR |
| Enzyme Length | 7 |
| Uniprot Accession Number | P86010 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate (DFP). {ECO:0000269|PubMed:17043825}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000305|PubMed:17043825}; |
| DNA Binding | |
| EC Number | 3.1.1.74 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:17043825). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:17043825). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (By similarity). {ECO:0000250|UniProtKB:P00590, ECO:0000269|PubMed:17043825}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (2) |
| Keywords | Direct protein sequencing;Hydrolase;Secreted;Serine esterase;Virulence |
| Interact With | |
| Induction | INDUCTION: By contact with cutin. {ECO:0000269|PubMed:17043825}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17043825}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17043825}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 881 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |