| IED ID | IndEnz0010001121 |
| Enzyme Type ID | esterase001121 |
| Protein Name |
Probable feruloyl esterase B-2 EC 3.1.1.73 Ferulic acid esterase B-2 FAEB-2 |
| Gene Name | faeB-2 AO090001000582 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MPSLRRLLPFLAAGSAALASQDTFQGKCTGFADKINLPNVRVNFVNYVPGGTNLSLPDNPTSCGTTSQVVSEDVCRIAMAVATSNSSEITLEAWLPQNYTGRFLSTGNGGLSGCIQYYDLAYTSGLGFATVGANSGHNGTSGEPFYHHPEVLEDFVHRSVHTGVVVGKQLTKLFYEEGFKKSYYLGCSTGGRQGFKSVQKYPNDFDGVVAGAPAFNMINLMSWSAHFYSITGPVGSDTYLSPDLWNITHKEILRQCDGIDGAEDGIIEDPSLCSPVLEAIICKPGQNTTECLTGKQAHTVREIFSPLYGVNGTLLYPRMQPGSEVMASSIMYNGQPFQYSADWYRYVVYENPNWDATKFSVRDAAVALKQNPFNLQTWDADISSFRKAGGKVLTYHGLMDQLISSENSKLYYARVAETMNVPPEELDEFYRFFQISGMAHCSGGDGAYGIGNQLVTYNDANPENNVLMAMVQWVEKGIAPETIRGAKFTNGTGSAVEYTRKHCRYPRRNVYKGPGNYTDENAWQCV |
| Enzyme Length | 526 |
| Uniprot Accession Number | Q2UMX6 |
| Absorption | |
| Active Site | ACT_SITE 188; /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); Beta strand (21); Chain (1); Disulfide bond (6); Glycosylation (9); Helix (27); Metal binding (5); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;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 | X-ray crystallography (1) |
| Cross Reference PDB | 6G21; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,747 |
| 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; METAL 266; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.73; |