| IED ID | IndEnz0010000661 |
| Enzyme Type ID | esterase000661 |
| Protein Name |
Cutinase EC 3.1.1.74 Cutin hydrolase |
| Gene Name | cutA |
| Organism | Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) |
| Enzyme Sequence | MKTSAQQLLSALLLPLSVLAAPTGSIEARACSDVTVIFARGTTETGTLGTVVGPPFLAALKSALGSSSVTMNGVDYPADVPGFLQGGDPAGSQTMATMVTSTLSSCPDTKLVISGYSQGGQLVHNAAKLLPAETTAKISSAVIFGDPDNGDPVQGVSADRTDIICHAGDNICQGGSLILLAHLTYGMDTTAAAAFVKKAAGL |
| Enzyme Length | 202 |
| Uniprot Accession Number | Q00298 |
| Absorption | |
| Active Site | ACT_SITE 117; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 169; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 182; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00590 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:9002270}; |
| 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:9002270). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:9002270). 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:9002270}. |
| 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 | INDUCTION: Induced during infection (PubMed:9002269, PubMed:9002270). By contact with cutin (PubMed:9002269, PubMed:9002270). Repressed by glucose (PubMed:9002269, PubMed:9002270). {ECO:0000269|PubMed:9002269, ECO:0000269|PubMed:9002270}. |
| 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 | 20,253 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |