Detail Information for IndEnz0005000602
IED ID IndEnz0005000602
Enzyme Type ID lipase000602
Protein Name Probable feruloyl esterase A
EC 3.1.1.73
Ferulic acid esterase A
Gene Name faeA An09g00120
Organism Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 niger Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Enzyme Sequence MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLCNIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTVTGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVSSPETTQYFRVTHSNDGIPNLPPAEQGYAHGGVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNDAHTTYFGMTSGACTW
Enzyme Length 281
Uniprot Accession Number A2QSY5
Absorption
Active Site ACT_SITE 154; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O42807; ACT_SITE 215; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O42807; ACT_SITE 268; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O42807
Activity Regulation
Binding Site BINDING 98; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O42807; BINDING 101; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O42807; BINDING 268; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O42807
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.; EC=3.1.1.73;
DNA Binding
EC Number 3.1.1.73
Enzyme Function FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Disulfide bond;Glycoprotein;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Serine esterase;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 30,550
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda