| IED ID | IndEnz0010000299 |
| Enzyme Type ID | esterase000299 |
| Protein Name |
Cutinase 1 EC 3.1.1.74 Cutin hydrolase 1 |
| Gene Name | CUTA |
| Organism | Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Glomerellales Glomerellaceae Colletotrichum Colletotrichum gloeosporioides species complex Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata) |
| Enzyme Sequence | MKFLSVLSLAITLAAAAPVEVETGVALETRQSSTRNELETGSSSACPKVIYIFARASTEPGNMGISAGPIVADALERIYGANNVWVQGVGGPYLADLASNFLPDGTSSAAINEARRLFTLANTKCPNAAIVSGGYSQGTAVMAGSISGLSTTIKNQIKGVVLFGYTKNLQNLGRIPNFETSKTEVYCDIADAVCYGTLFILPAHFLYQTDAAVAAPRFLQARIG |
| Enzyme Length | 224 |
| Uniprot Accession Number | P11373 |
| Absorption | |
| Active Site | ACT_SITE 136; /note=Nucleophile; /evidence=ECO:0000305|PubMed:18983850; ACT_SITE 191; /evidence=ECO:0000305|PubMed:18983850; ACT_SITE 204; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:18983850 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate (DFP). {ECO:0000269|PubMed:17043825}. |
| 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, ECO:0000305|PubMed:17043825}; |
| 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:17043825). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:17043825). 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:17043825}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (5); Chain (1); Disulfide bond (2); Helix (10); Mutagenesis (1); Sequence conflict (2); Signal peptide (1); Site (2); Turn (3) |
| Keywords | 3D-structure;Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal;Virulence |
| Interact With | |
| Induction | INDUCTION: By contact with cutin. {ECO:0000269|PubMed:17043825}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17043825}. |
| 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}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17043825}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3DCN; 3DD5; 3DEA; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,477 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |