| IED ID | IndEnz0010001273 |
| Enzyme Type ID | esterase001273 |
| Protein Name |
Probable feruloyl esterase B-2 EC 3.1.1.73 Ferulic acid esterase B-2 FAEB-2 |
| Gene Name | faeB-2 AFUA_6G09040 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MTKLSLLPLLTLASAVLAKQDAFQAKCASFGRKIKLPNVHVNFVEYVPGGTNLTLPDNDVTCGASSQVVSADMCRVAMAVDTSKSSQITLEAWFPREYTGRFLSTGNGGLSGCIQYYDLAYTAGLGFATVGANNGHNGTSGKPFYQHPEVIEDFAYRSIHTGVVVGKQLTKMFYKEGFDKSYYLGCSTGGRQGFKSIQKYPNDFDGVVAGAPAFNFVNLISWSIHFYSITGSNTSDTYLSPESWKVVHDEIVRQCDEIDGAKDGIIEDTDLCQPVIETIICKPGASDKTNCITGAQAKTVRNVLSPFYGVNGNLLYPRMQPGSELFASSVVYNGQPFRYSTDWYRYVVYNNPDWDATKWTVEDAAVALAQNPYNIQTWDADISSFQKAGGKVLTYHGMQDQLISSDNSKLYYARVAEEMGLGPEELDDFYRFFPVSGMAHCTGGDGAYGIGNGLRTYNGAEPENNVLMAMVQWVEKGIAPEFIRGAKFSNGVGSSVEYTRKHCRYPRRNVYKGPGNYSDENAWECV |
| Enzyme Length | 526 |
| Uniprot Accession Number | Q4WMR0 |
| 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 | 57,865 |
| 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 |