IED ID | IndEnz0010001196 |
Enzyme Type ID | esterase001196 |
Protein Name |
Probable feruloyl esterase B EC 3.1.1.73 Ferulic acid esterase B FAEB |
Gene Name | faeB ACLA_083360 |
Organism | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
Enzyme Sequence | MARLSLLTLLALGSAALAKKDTFQTKCAALQHKVKLPNVHVNFVEYVPGGTNLDLPDNAPSCGASSQAVSTDMCRIAMAVDTSDSSQITLEAWFPRDYTGRFLSTGNGGLSGCIQYYDLAYAAGLGFATVGANNGHNGTSGEPFYQHPEVVEDFAHRSVHTGVVVGKQLTKLFYDKGFKKSYYLGCSTGGRQGFKSVQKYPKDFDGIVAGAPAFNFVNLISWSAYFYSLTGSNTSESYLSPAMWKIAHDEIVRQCDELDGAKDGIIEDTDLCHPRLETIICKPGAKDTANCLTGAQAKTVRDVLSPMYGVNGTLLYPRMQPGSEVYAAGIMYNGEPFQYSTDWYRYVVYNNPDWDDTKWSVEDAAAALAQNPYDIQTFDADISSFRGAGGKVLTYHGLQDQMISSDNSKLYYARVAETMKLPPSELDEFYRFFPVSGMTHCAGGDGAYGIGNGLGSYNGVDPENNVLMAMVQWVEKGIAPEFIRGAKFAEGPGSAVEYTRKHCRYPRRNVYKGPGNYTDENAWECV |
Enzyme Length | 526 |
Uniprot Accession Number | A1CTK4 |
Absorption | |
Active Site | ACT_SITE 187; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 400; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 440; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
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:0000250|UniProtKB:Q8WZI8}; |
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. {ECO:0000250|UniProtKB:Q8WZI8}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (6); Glycosylation (4); Metal binding (5); Signal peptide (1) |
Keywords | Calcium;Carbohydrate metabolism;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Polysaccharide degradation;Reference proteome;Secreted;Serine esterase;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 57,522 |
Kinetics | |
Metal Binding | METAL 256; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 259; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 261; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 263; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 265; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
Rhea ID | |
Cross Reference Brenda |