IED ID | IndEnz0012000001 |
Enzyme Type ID | hemicellulase000001 |
Protein Name |
Feruloyl esterase B EC 3.1.1.73 Cinnamoyl ester hydrolase Esterase A EstA Ferulic acid esterase B |
Gene Name | ESTA |
Organism | Piromyces equi |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Chytridiomycota Chytridiomycota incertae sedis Neocallimastigomycetes Neocallimastigales Neocallimastigaceae Piromyces unclassified Piromyces Piromyces equi |
Enzyme Sequence | MKTSIVLSIVALFLTSKASADCWSERLGWPCCSDSNAEVIYVDDDGDWGVENNDWCGIQKEEENNNSWDMGDWNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGGMPWGDFGGNQGGGMPWGDFGGNQGGNQGGGMPWGDFGGNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGGMQWGDFGGNQGGNQDWGNQGGNSGPTVEYSTDVDCSGKTLKSNTNLNINGRKVIVKFPSGFTGDKAAPLLINYHPIMGSASQWESGSQTAKAALNDGAIVAFMDGAQGPMGQAWNVGPCCTDADDVQFTRNFIKEITSKACVDPKRIYAAGFSMGGGMSNYAGCQLADVIAAAAPSAFDLAKEIVDGGKCKPARPFPILNFRGTQDNVVMYNGGLSQVVQGKPITFMGAKNNFKEWAKMNGCTGEPKQNTPGNNCEMYENCKGGVKVGLCTINGGGHAEGDGKMGWDFVKQFSLP |
Enzyme Length | 536 |
Uniprot Accession Number | Q9Y871 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by the specific serine esterase inhibitor AEBSF. |
Binding Site | |
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 of the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin. {ECO:0000269|PubMed:10493932}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (1); Domain (1); Glycosylation (1); Region (4); Repeat (12); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Glycoprotein;Hydrolase;Polysaccharide degradation;Repeat;Secreted;Serine esterase;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 55,540 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.1.1.73; |