IED ID | IndEnz0010001490 |
Enzyme Type ID | esterase001490 |
Protein Name |
Feruloyl esterase D EC 3.1.1.73 Ferulic acid esterase D FAE |
Gene Name | faeD-3.544 NCU08785 |
Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora Neurospora crassa Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Enzyme Sequence | MAGLHSRLTTFLLLLLSALPAIAAAAPSSGCGKGPTLRNGQTVTTNINGKSRRYTVRLPDNYNQNNPYRLIFLWHPLGSSMQKIIQGEDPNRGGVLPYYGLPPLDTSKSAIYVVPDGLNAGWANQNGEDVSFFDNILQTVSDGLCIDTNLVFSTGFSYGGGMSFSLACSRANKVRAVAVISGAQLSGCAGGNDPVAYYAQHGTSDGVLNVAMGRQLRDRFVRNNGCQPANGEVQPGSGGRSTRVEYQGCQQGKDVVWVVHGGDHNPSQRDPGQNDPFAPRNTWEFFSRFN |
Enzyme Length | 290 |
Uniprot Accession Number | Q7RWX8 |
Absorption | |
Active Site | |
Activity Regulation | |
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:14595525}; |
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 as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin (By similarity). Active against methyl esters of ferulate (MFA), sinapate (MSA), caffeate (MCA) and p-coumarate (MpCA) (PubMed:14595525). {ECO:0000250|UniProtKB:O42807, ECO:0000269|PubMed:14595525}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Region (1); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Serine esterase;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42807}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 31,146 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |