| IED ID | IndEnz0010001931 |
| Enzyme Type ID | esterase001931 |
| Protein Name |
Probable feruloyl esterase B EC 3.1.1.73 Ferulic acid esterase B FAEB |
| Gene Name | faeB AN1772 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MALLRHLLPVLTVGSAVQSAVLVQDQFQTRCENFAGKIDLPNVKVNFASYIPGSTNLTLDNVPTCDQSQVVSSDICRVAMAVTTSNASEITLEAWFPRDYTGRFLSTGNGGLGGCIQYSDLDYASRLGFATVGANNGHNGTSGEPFYKAPEVLEDFVYRSVHTGIVVGKQLTKLFYDEGFDTSYYLGCSTGGRQGFKLAQDFPGEVDGIIAGAPAINFVGLLSWSAHFYPITGPVGSATYLSLDDWDLVHEEILRQCDGLDGAEDGIIEDPDLCHPNATTLLCSPGATSGSCLTATQVNTVHEVYAPLLSSNSTLIYPRMQPGGEQFAAPAMYNGQPFQYSKDWWRYVVYSDPTWNATKWTIRDAEAALRQNPYNIQTWNADLSPLRDSGSKLLTYHGLQDQLISSDDSKLYYHRLMKTMGVTSNQLDEFYRFFQISGMAHCQDGDGAYGIGNRAETEFSTEPEDNVLMAMVRWVEEGIAPETVRGAKFSDGVGSEVEYYRKHCRYPRRNVYKGPGDYTDETAWECV |
| Enzyme Length | 527 |
| Uniprot Accession Number | Q5BCF8 |
| Absorption | |
| Active Site | ACT_SITE 189; /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 (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..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,095 |
| Kinetics | |
| Metal Binding | METAL 258; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 261; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 263; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 265; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 267; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.73; |