Detail Information for IndEnz0010000809
IED ID IndEnz0010000809
Enzyme Type ID esterase000809
Protein Name Probable cutinase 2
EC 3.1.1.74
Cutin hydrolase 2
Gene Name AFUB_071270
Organism Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (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 CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Enzyme Sequence MNLRLLTLALAGLAAASPVAIEERQLSSGNELRNGACKPITFIFARASTEPGLMGLSTGPAVCNSLKAAKPGQVACQGVGPAYTADLASNALPENTSQAAINEAMELFKQAASKCPDTQIVAGGYSQGTAVMDGSIKRLPEEVKERIKGVVLFGYTRNAQERGQIANFPKDKVKIYCAMGDLVCDGTLIVTAAHFTYGANTGDAARFLLGKLTA
Enzyme Length 214
Uniprot Accession Number B0Y537
Absorption
Active Site ACT_SITE 126; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 181; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 194; /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;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..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,326
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda