| IED ID | IndEnz0010001366 |
| Enzyme Type ID | esterase001366 |
| Protein Name |
Cutinase 1 EC 3.1.1.74 Ancut1 Cutin hydrolase 1 |
| Gene Name | cut1 AN5309 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MKLQLHLALSLLAAIVAANPIRLDQRQITGNELRDGSCHDVTFIFARGSTELGYLGSTVGPATCNVLKLRKPGQVACQGVAPAYIADLASNFLPQGTNQIAINEAKSLFELAASKCPNTKIVAGGYSQGAAVMHAAISTLSSTVQDQIKGVVLFGDTRNKQDGGRIPNFPTDKTKIICAFGDLVCEGTLVITAAHLSYIDDVPDAADFLVGKL |
| Enzyme Length | 213 |
| Uniprot Accession Number | Q5B2C1 |
| Absorption | |
| Active Site | ACT_SITE 127; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 182; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 195; /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). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (Probable). {ECO:0000250|UniProtKB:Q5AVY9, ECO:0000305|PubMed:25043916}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Signal peptide (1); Site (2) |
| Keywords | Disulfide bond;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Induced during growth on cutin, in a manner dependent on transcription factors FarA and FarB (PubMed:30863878). Induced during growth on suberin (PubMed:25043916). Induced during growth on the lipidic carbon sources 16-hydroxyhexadecanoic acid and propyl ricinoleate (synthetic cutin monomers), triacetin and triesterate (triglycerides), and olive oil (PubMed:30863878). Repressed during growth on glucose (PubMed:30863878). {ECO:0000269|PubMed:25043916, ECO:0000269|PubMed:30863878}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25043916}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,413 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |