IED ID | IndEnz0010000455 |
Enzyme Type ID | esterase000455 |
Protein Name |
Feruloyl esterase A EC 3.1.1.73 Ferulic acid esterase A |
Gene Name | faeA |
Organism | Aspergillus tubingensis |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus tubingensis |
Enzyme Sequence | MKQFSAKYAIAVVVTAGHALAASTQGISEDLYSRLVEMATISQAAYADLCNIPSTIIKGEKIYNSQTDINGWILRDDSSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNSCEVHGGYYIGWISVQDQVESLVQQQVSQFPDYALTVTGHSLGASLAALTAAQLSATYDNIRLYTFGEPRSNQAFASYMNDAFQASSPDTTQYFRVTHANDGIPNLPPADEGYAHGVVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNNAHTTYFGMTSGHCTW |
Enzyme Length | 280 |
Uniprot Accession Number | O42815 |
Absorption | |
Active Site | ACT_SITE 154; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O42807; ACT_SITE 214; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O42807; ACT_SITE 267; /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 267; /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. {ECO:0000269|PubMed:9406381}. |
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;Secreted;Serine esterase;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9406381}. |
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 | 30,451 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.1.1.73; |