| IED ID | IndEnz0004000021 |
| Enzyme Type ID | xylanase000021 |
| Protein Name |
Endo-1,4-beta-xylanase/feruloyl esterase Includes: Endo-1,4-beta-xylanase EC 3.2.1.8 ; Feruloyl esterase EC 3.1.1.73 Ferulic acid esterase |
| Gene Name | xyn10D-fae1A PRU_2728 ORF02827 |
| Organism | Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Prevotellaceae Prevotella Prevotella ruminicola (Bacteroides ruminicola) Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) |
| Enzyme Sequence | MKKLLVALSLIAGSLTASAQWGRPVDYAAGPGLKDAYKDYFTVGVAVNKFNISDPAQTAIVKKQFNSVTAENAWKPGEIHPKEGVWNFGLADSIANFCRENGIKMRGHCLCWHSQFADWMFTDKKGKPVKKEVFYQRLREHIHTVVNRYKDVVYAWDVVNEAMADDGRPFEFVDGKMVPASPYRQSRHFKLCGDEFIAKAFEFAREADPTGVLMYNDYSCVDEGKRERIYNMVKKMKEAGVPIDGIGMQGHYNIYFPDEEKLEKAINRFSEIVNTIHITELDLRTNTESGGQLMFSRGEAKPQPGYMQTLQEDQYARLFKIFRKHKDVIKNVTFWNLSDKDSWLGVNNHPLPFDENFKAKRSLQIIRDFDAAMDNRKPKEDFVPNPMNQPGQEYPMVNSEGYARFRVEAPDAKSVIVSLGLGGRGGTVLRKDKNGVWTGTTEGPMDPGFHYYHLTIDGGVFNDPGTHNYFGSCRWESGIEIPAKDQDFYAYRKDINHGNIQQVTFWSESTGKMQTANVYLPYGYGKVVKGKQERYPVLYLQHGWGENETSWPVQGKAGLIMDNLIADGKIKPFIVVMAYGLTNDFKFGSIGKFTAEEFEKVLIDELIPTIDKNFLTKADKWNRAMAGLSMGGMETKLITLRRPEMFGYWGLLSGGTYMPEEIKDPKAVKYIFVGCGDKENPEGINKSVEALKAAGFKAEGLVSEGTAHEFLTWRRCLEKMAQSLFK |
| Enzyme Length | 726 |
| Uniprot Accession Number | D5EY13 |
| Absorption | |
| Active Site | ACT_SITE 161; /note=Proton donor; for xylanase activity; /evidence=ECO:0000250; ACT_SITE 280; /note=Nucleophile; for xylanase activity; /evidence=ECO:0000305|PubMed:19304844; ACT_SITE 629; /note=Nucleophile; for esterase activity; /evidence=ECO:0000305|PubMed:19304844 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}; CATALYTIC ACTIVITY: Reaction=Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}; |
| DNA Binding | |
| EC Number | 3.2.1.8; 3.1.1.73 |
| Enzyme Function | FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has endo-xylanase activity towards substrates such as oat spelt xylan (OSX), acetylated xylo-oligosaccharides and acetylated xylan, producing primarily xylobiose; cannot hydrolyze xylobiose to xylose. Also has feruloyl esterase activity, releasing ferulic acid from methylferulate, and from the more natural substrates wheat bran, corn fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters. Exhibits negligible acetyl esterase activity on sugar acetates. Acts synergistically with Xyl3A to increase the release of xylose from xylan. Does not possess endoglucanase or mannanase activities since it is not able to hydrolyze carboxymethyl cellulose and locust bean gum. {ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for xylanase activity. {ECO:0000269|PubMed:19304844}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Mutagenesis (2); Region (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Reference proteome;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: By growth on ester-enriched corn oligosaccharides. {ECO:0000269|PubMed:21742923}. |
| Subcellular Location | |
| 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 | 82,289 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |