Detail Information for IndEnz0010000298
IED ID IndEnz0010000298
Enzyme Type ID esterase000298
Protein Name Probable cutinase 1
EC 3.1.1.74
Cutin hydrolase 1
Gene Name AFLA_039350
Organism Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus flavus Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Enzyme Sequence MVMLRSLLVSALAALAAASPIAEPADQSLEARQLGSSNDLTNGACKDVTLIFARGSTEMGNMGTVIGPPLCSALKSKLGADKVACQGVGGLYTGGLMQNALPQNTDPGAISTAKSLFEQASTKCPNTQIVAGGYSQGSAVIDNAVQQLSAEVKDKVKGVVFFGFTRNLQDKGQIPNYPKDNVKVFCAMGDLVCDGTLIVTAAHLTYTINAPEAASFLASKVQSA
Enzyme Length 224
Uniprot Accession Number B8NCM8
Absorption
Active Site ACT_SITE 135; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 190; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 203; /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 23,073
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda