| IED ID | IndEnz0010001091 |
| Enzyme Type ID | esterase001091 |
| Protein Name |
Cutinase CUT1 EC 3.1.1.74 Cutin hydrolase |
| Gene Name | CUT1 MGG_01943 |
| Organism | Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Pyriculariaceae Pyricularia Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae) Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) |
| Enzyme Sequence | MQFITVALTLIALASASPIATNVEKPSELEARQLNSVRNDLISGNAAACPSVILIFARASGEVGNMGLSAGTNVASALEREFRNDIWVQGVGDPYDAALSPNFLPAGTTQGAIDEAKRMFTLANTKCPNAAVVAGGYSQGTAVMFNAVSEMPAAVQDQIKGVVLFGYTKNLQNRGRIPDFPTEKTEVYCNASDAVCFGTLFLLPAHFLYTTESSIAAPNWLIRQIRAA |
| Enzyme Length | 228 |
| Uniprot Accession Number | P30272 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 193; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 206; /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:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109}; |
| 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). Required for efficient penetration of the host plant cuticle by the appressorium during the initial stage of fungal infection (By similarity). {ECO:0000250|UniProtKB:G4MZV6}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (1); Natural variant (1); Signal peptide (1); Site (2) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Reference proteome;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..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,192 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |