Detail Information for IndEnz0010001230
IED ID IndEnz0010001230
Enzyme Type ID esterase001230
Protein Name Probable cutinase 3
EC 3.1.1.74
Cutin hydrolase 3
Gene Name AFUB_099910
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 MSLRSLFVAGLATLALAVPAPQIQARQGMSSNELESGPCRDVTFIFARGSTEQGNMGLIVGPGVCSSLKKDLGSDKVACQGVGGAYTAQLAPNFLSQNTNQASINAATDMFDLANTKCPNTKIVAGGYSQGSAVIDNTIQALGSDLKAKVKGVVLFGFTRNVADKGQIPGYPKDQTKIYCAVGDMVCVNTLIITPAHLTYGADAGDAAKFLASKVQE
Enzyme Length 217
Uniprot Accession Number B0YEP5
Absorption
Active Site ACT_SITE 129; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10108; ACT_SITE 184; /evidence=ECO:0000255|PROSITE-ProRule:PRU10108; ACT_SITE 197; /note=Proton donor/acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10108
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};
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;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..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,483
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda