| IED ID | IndEnz0010001287 |
| Enzyme Type ID | esterase001287 |
| Protein Name |
Feruloyl esterase C EC 3.1.1.73 Ferulic acid esterase C FAE |
| Gene Name | faeC TSTA_065520 |
| Organism | Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces stipitatus Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum) |
| Enzyme Sequence | MMLTSAILLLTLGVQLSHADDSSRENFSNRCDQLAKEIHIPNVTVNFVEYVANGTNVTLADNPPSCGQSNQVVLADLCRVAMEVTTSNQSQITLEAWFPENYTGRFLSTGNGGLAGCIQYVDMAYASSMGFATVGANGGHNGTSGESFYHNPDIVEDLSWRSVHTGVVVGKELTKKFYHEGFHKSYYLGCSTGGRQGFKAVQEFVHDFDGVVAGCPAFNFVNLNSWSGHFYPITGNSSADTFLTTAQWTLVQQSVMEQCDSLDGAVDGVIEAIDQCHPVFEQLICRPGQNASECLTGKQVNTAQLVLSPIYGTKGEFLYPRMQPGVENVDMYITYNGDPFAYSTDWYKYVVFSDPNWDPATLNAQDYEIALAQNPSNIQTFEGDLSAFRDAGAKVLTYHGTADPIITGETSKVYYRHVAETMNAAPEELDEFYRYFRIGGMSHCGGGTGATAIGNVLSAQWSNDPDANVLMAMVRWVEEGVAPEYIRGASLGSGPGAKVEYTRRHCKYPTRNVYVGPGNWTDENAWKCIL |
| Enzyme Length | 530 |
| Uniprot Accession Number | B8LV47 |
| Absorption | |
| Active Site | ACT_SITE 191; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 403; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 443; /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:0000269|PubMed:15006424}; |
| 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 (By similarity). Active against methyl esters of sinapate (MSA) and caffeate (MCA) (PubMed:15006424). {ECO:0000250|UniProtKB:O42807, ECO:0000269|PubMed:15006424}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Metal binding (5); Signal peptide (1) |
| Keywords | Calcium;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Polysaccharide degradation;Reference proteome;Secreted;Serine esterase;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42807}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,020 |
| Kinetics | |
| Metal Binding | METAL 260; /note=Calcium; /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; METAL 267; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 269; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.73; |