| IED ID | IndEnz0010000721 |
| Enzyme Type ID | esterase000721 |
| Protein Name |
Cutinase EC 3.1.1.74 Cutin hydrolase |
| Gene Name | CUTA |
| Organism | Colletotrichum truncatum (Anthracnose fungus) (Colletotrichum capsici) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Glomerellales Glomerellaceae Colletotrichum Colletotrichum truncatum species complex Colletotrichum truncatum (Anthracnose fungus) (Colletotrichum capsici) |
| Enzyme Sequence | MKFLSIISLAVSLVAAAPVEVGLDTGVANLEARQSSTRNELESGSSSNCPKVIYIFARASTEPGNMGISAGPIVADALESRYGASQVWVQGVGGPYSADLASNFIIPEGTSRVAINEAKRLFTLANTKCPNSAVVAGGYSQGTAVMASSISELSSTIQNQIKGVVLSAITKNLQNLGRIPNFSTSKTEVYCALADAVCYGTLFILPAHFLYQADAATSAPRFLAARIG |
| Enzyme Length | 228 |
| Uniprot Accession Number | P10951 |
| Absorption | |
| Active Site | ACT_SITE 140; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 195; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 208; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00590 |
| Activity Regulation | ACTIVITY REGULATION: Partially inhibited by berberine; higher inhibitory effects are observed with longer chain polyester substrates. {ECO:0000269|PubMed:33606796}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:33606796}; |
| 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:33606796). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:33606796). 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:33606796}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Signal peptide (1); Site (2) |
| Keywords | Direct protein sequencing;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:0000305|Ref.1}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,714 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |