| IED ID | IndEnz0010000862 |
| Enzyme Type ID | esterase000862 |
| Protein Name |
Cutinase CUT2 EC 3.1.1.74 |
| Gene Name | CUT2 MGG_09100 |
| 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 | MQFSLSIATAILAATASAMPVLETRQTVGTTANEFTSGGCKDVVLLYARGTTQAGNMGQEPGPELGNALKARLGAARVAVQGVAYSASLLGNLNPGGAPANEATSFRTLIGQVASQCPNARIVVSGYSQGAALVHRAVEGATAAVRARIAAGVTFGDTQKQQDGGRIPGLDASKTLIICNTGDRVCEGTLIITAAHSGYGARAGEAVDFIAARV |
| Enzyme Length | 214 |
| Uniprot Accession Number | G4MZV6 |
| Absorption | |
| Active Site | ACT_SITE 128; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 183; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 196; /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|RuleBase:RU361263, ECO:0000305|PubMed:17704215}; |
| 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:17704215). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:17704215). Required for efficient penetration of the host plant cuticle by the appressorium during the initial stage of fungal infection (PubMed:17704215). {ECO:0000269|PubMed:17704215}. |
| 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;Reference proteome;Secreted;Serine esterase;Signal;Virulence |
| Interact With | |
| Induction | INDUCTION: Induced during infection; levels are increased during germ tube and appressorium differentiation, and during penetration. {ECO:0000269|PubMed:17704215}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17704215}. |
| 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..18; /evidence=ECO:0000255|RuleBase:RU361263 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,602 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |