IED ID | IndEnz0010001260 |
Enzyme Type ID | esterase001260 |
Protein Name |
Probable cutinase 1 EC 3.1.1.74 Cutin hydrolase 1 |
Gene Name | AFUA_2G09380 |
Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Enzyme Sequence | MKFALLSLAAMAVASPVAIDVRQTAITGDELRTGPCEPITFIFARGSTEPGLLGITTGPGVCNALKLSRPGQVACQGVGPAYIADLASNFLPQGTSQVAIDEAAGLFKLAASKCPDTKIVAGGYSQGAAVMHGAIRNLPSNVQNMIKGVVLFGDTRNKQDGGRIPNFPTDRTKIYCAFGDLVCDGTLIITPAHLSYGDDVPSATSFLLSKV |
Enzyme Length | 211 |
Uniprot Accession Number | Q4X1N0 |
Absorption | |
Active Site | ACT_SITE 125; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 180; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 193; /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). {ECO:0000250|UniProtKB:P00590}. |
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 | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}. |
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 | 21,856 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |