| IED ID | IndEnz0010000501 |
| Enzyme Type ID | esterase000501 |
| Protein Name |
Cutinase EC 3.1.1.74 Cutin hydrolase |
| Gene Name | CUT1 |
| Organism | Monilinia fructicola (Brown rot fungus) (Ciboria fructicola) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Monilinia Monilinia fructicola (Brown rot fungus) (Ciboria fructicola) |
| Enzyme Sequence | MKTSAQQLLSLLLLPLSAIAAPTGEIEARACSTVTVIFARGTTETPTLGTVIGPQFLAALKSSFGGSVTMNGVPYAADVPGFLKGGDPTGSKVMANMVSSALSSCPNTKLVISGYSQGGQLVHNAAKQLPAATTAKIAAAVIFGDPDNGSPVQGVPAAKTKIICHAGDNICQHGSMILMPHLTYGMDATAAAAFVKQVAGS |
| Enzyme Length | 201 |
| Uniprot Accession Number | Q8TGB8 |
| Absorption | |
| Active Site | ACT_SITE 116; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10108; ACT_SITE 168; /evidence=ECO:0000255|PROSITE-ProRule:PRU10108; ACT_SITE 181; /note=Proton donor/acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10108 |
| Activity Regulation | |
| 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}; |
| 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 (By similarity). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity). 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Signal peptide (1); Site (1) |
| Keywords | Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}. |
| Modified Residue | |
| Post Translational Modification | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 20,227 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |