| IED ID | IndEnz0010000003 |
| Enzyme Type ID | esterase000003 |
| Protein Name |
Feruloyl esterase B EC 3.1.1.73 Cinnamoyl esterase Ferulic acid esterase B FAEB |
| Gene Name | FAEB |
| Organism | Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Enzyme Sequence | MAIPLVLVLAWLLPVVLAASLTQVNNFGDNPGSLQMYIYVPNKLASKPAIIVAMHPCGGSATEYYGMYDYHSPADQYGYILIYPSATRDYNCFDAYSSASLTHNGGSDSLSIVNMVKYVISTYGADSSKVYMTGSSSGAIMTNVLAGAYPDVFAAGSAFSGMPYACLYGAGAADPIMSNQTCSQGQIQHTGQQWAAYVHNGYPGYTGQYPRLQMWHGTADNVISYADLGQEISQWTTIMGLSFTGNQTNTPLSGYTKMVYGDGSKFQAYSAAGVGHFVPTDVSVVLDWFGITSGTTTTTTPTTTPTTSTSPSSTGGCTAAHWAQCGGIGYSGCTACASPYTCQKANDYYSQCL |
| Enzyme Length | 353 |
| Uniprot Accession Number | Q9HE18 |
| Absorption | |
| Active Site | ACT_SITE 136; /note=Charge relay system |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the specific serine esterase inhibitor AEBSF. {ECO:0000269|PubMed:11082184}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:11082184}; |
| 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 and feruloyl-arabinose ester bonds in pectin. Binds strongly to cellulose. {ECO:0000269|PubMed:11082184}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (2); Region (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycoprotein;Hydrolase;Polysaccharide degradation;Secreted;Serine esterase;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Repressed by glucose, probably via the carbon catabolite repressor protein CreA. {ECO:0000269|PubMed:11082184, ECO:0000303|PubMed:11082184}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11082184}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000303|PubMed:11082184, ECO:0000305}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:11082184 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,334 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.73; |