Detail Information for IndEnz0010001184
IED ID IndEnz0010001184
Enzyme Type ID esterase001184
Protein Name Probable cutinase 1
EC 3.1.1.74
Cutin hydrolase 1
Gene Name NFIA_084890
Organism Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Enzyme Sequence MKFALLSLAAMAVASPVAIDVRQTAIAGDELRTGPCEPITFIFARGSTEPGLLGITTGPGVCNALKLSRPGQVACQGVGPAYIADLASNFLPQGTNQIAIDEAAGLFKLAASKCPNTKIVAGGYSQGAAVMHGAIRNLPSDVQNMIKGVVLFGDTRNKQDGGRIPNFPTDRTKIYCAFGDLVCDGTLIITAAHLSYGDDVPNATSFLLSKV
Enzyme Length 211
Uniprot Accession Number A1DGN0
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); Glycosylation (1); Signal peptide (1); Site (2)
Keywords Disulfide bond;Glycoprotein;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 21,868
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda