| IED ID | IndEnz0010000001 |
| Enzyme Type ID | esterase000001 |
| Protein Name |
Feruloyl esterase A EC 3.1.1.73 Cinnamoyl esterase FAE-III Ferulic acid esterase A |
| Gene Name | faeA |
| Organism | Aspergillus niger |
| 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 |
| Enzyme Sequence | MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLCNIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTVTGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVSSPETTQYFRVTHSNDGIPNLPPADEGYAHGGVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNDAHTTYFGMTSGACTW |
| Enzyme Length | 281 |
| Uniprot Accession Number | O42807 |
| Absorption | |
| Active Site | ACT_SITE 154; /note=Nucleophile; /evidence=ECO:0000269|PubMed:15081808; ACT_SITE 215; /note=Charge relay system; /evidence=ECO:0000305|PubMed:15103133; ACT_SITE 268; /note=Charge relay system; /evidence=ECO:0000305|PubMed:15103133 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the specific serine esterase inhibitor diisopropylfluorophosphate. {ECO:0000269|PubMed:9649839}. |
| Binding Site | BINDING 98; /note=Substrate; /evidence=ECO:0000269|PubMed:16128806; BINDING 101; /note=Substrate; /evidence=ECO:0000269|PubMed:16128806; BINDING 268; /note=Substrate; /evidence=ECO:0000269|PubMed:16128806 |
| 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. Binds to cellulose. {ECO:0000269|PubMed:11931668, ECO:0000269|PubMed:15081808, ECO:0000269|PubMed:17027758, ECO:0000269|PubMed:7805053, ECO:0000269|PubMed:9406381, ECO:0000269|PubMed:9649839, ECO:0000269|Ref.5}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-60 degrees Celsius. {ECO:0000269|PubMed:17027758}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:17027758}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Helix (10); Mutagenesis (3); Sequence conflict (19); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Polysaccharide degradation;Secreted;Serine esterase;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: By xylose and arabinose, probably via the xylanolytic transcriptional activator XlnR. By ferulic acid, vanillic acid and other aromatic residues with the following substituants on the aromatic ring: a methoxy group at C-3, a hydroxy group at C-4 and an unsubstituted C-5. Repressed by simple sugars, probably via the carbon catabolite repressor protein CreA. {ECO:0000269|PubMed:10584009, ECO:0000269|PubMed:11931668}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9406381, ECO:0000269|Ref.5}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000305|PubMed:17027758}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:9406381 |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1USW; 1UWC; 1UZA; 2BJH; 2HL6; 2IX9; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,537 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for methyl ferulate {ECO:0000269|PubMed:17027758}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.73; |