| IED ID | IndEnz0010000524 |
| Enzyme Type ID | esterase000524 |
| Protein Name |
Probable feruloyl esterase B-1 EC 3.1.1.73 Ferulic acid esterase B-1 FAEB-1 |
| Gene Name | faeB-1 NFIA_047590 |
| Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| 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 fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Enzyme Sequence | MMRWFLLIGLASAAATDSSASFESRCQHFHKEIHLQNVHVHSTTYVPIGSNISMAYNPPICGGTSSSSISTIEFCQVALNVTTSDKSQFFMEAWLPSNYTGRFLSTGNGGLNGCVGYGDMIYASQYGFATIGTNNGHFGDTGQYFLNNPEVIEDFAYRALHTGTVVGKALTKLFYPQGYKNSYYLGCSTGGRQGWKSIQRFPDDFDGVVAGAPAFNFVNLCNWGSRFLKITGPPDSDTFVTSAQWSIIHNEIIRQCDALDGAVDGTIEDTDLCQPIFETLICNSTAVNKTSCLTGVQANTVNEVFSAMYGLDGKWLYPRMQPGSELAASFIYYSGNGFKYSDDWFKYVVYNDSNWDHSTWTLADAAAADAQDPFQISTFDGDISGFQKAGGKVLHYHGLEDAIITSDSSKAYYKHVADTMGLSPSDLDQFYRFFPISGMGHCSPGTGAASIGQGSSTYAGDDPQDNVLMAMVQWVEKGIAPEYVRGSKKSIDGQTEYRRKHCKYPKRNRYVGPGKYTDENAWKCV |
| Enzyme Length | 525 |
| Uniprot Accession Number | A1DKV3 |
| Absorption | |
| Active Site | ACT_SITE 188; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 401; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 441; /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 (6); Metal binding (4); 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..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,678 |
| Kinetics | |
| Metal Binding | METAL 257; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 260; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 262; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 264; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
| Rhea ID | |
| Cross Reference Brenda |