| IED ID | IndEnz0004000195 |
| Enzyme Type ID | xylanase000195 |
| Protein Name |
Xylan 1,4-beta-xylosidase EC 3.2.1.37 1,4-beta-D-xylan xylohydrolase Alpha-L-arabinofuranosidase Arabinosidase EC 3.2.1.55 Beta-D-xylosidase Exo-1,4-beta-xylosidase |
| Gene Name | xyl3A PRU_2730 02829 |
| 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 | MKYQLFLSLALCVGLGASAQTLPYQNPNLSAKERAVDLCSRLTLEEKAMLMLDESPAIPRLGIKKFFWWSEALHGAANMGNVTNFPEPVGMAASFNPHLLFKVFDIASTEFRAQYNHRMYDLNGEDMKMRSLSVWTPNVNIFRDPRWGRGQETYGEDPYLTSVMGVQVVKGLQGPEDARYRKLWACAKHYAVHSGPEYTRHTANLTDVSARDFWETYMPAFKTLVKDAKVREVMCAYQRLDDDPCCGSTRLLQQILRDEWGFEYLVVSDCGAVSDFYENHKSSSDAVHGTSKAVLAGTDVECGFNYAYKSLPEAVRKGLLSEKEVDKHVIRLLEGRFDLGEMDDPSLVEWSKIPYSAMSTKASANVALDMARQTIVLLQNKNNILPLKKNAEKIAIIGPNAHNEPMMWGNYNGTPNHTVTILDGVKAKQKKLVYIPGCDLTNDKVMECHLATDCVTPDGKKGLKGTFWNNTEMAGKPFTTEYYTKPVNVTTAGMHVFAPNLPIEDFSAKYETTFTAKEAGEYVVNVESTGHFELYVNGKQQFVNHIWRATPTRTVLKAEKGQKFDIEVRFQTVKTWGASMKIDVARELNIDYQETIAQLKGINKVIFCGGIAPSLEGEEMPVNIEGFKGGDRTSIELPKVQREFLKALKAAGKQVIYVNCSGSAIALQPETESCDAIVQAWYPGQEGGTAVADVLFGDYNPGGKLSVTFYKNDQQLPDYEDYSMKGRTYRYFDDALFPFGYGLSYTTFEVGEAKVEAATDGALYNVQIPVTNTGTKNGSETIQLYIRNLQDPDGPLKSLRGFERLDIKAGKTATANLKLTKESLEFWDAETNTMRTKPGKYEILYGTSSLDKDLKKLTITL |
| Enzyme Length | 861 |
| Uniprot Accession Number | D5EY15 |
| Absorption | |
| Active Site | ACT_SITE 269; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 616; /note=Proton donor/acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.; EC=3.2.1.37; Evidence={ECO:0000269|PubMed:19304844}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55; Evidence={ECO:0000269|PubMed:19304844}; |
| DNA Binding | |
| EC Number | 3.2.1.37; 3.2.1.55 |
| Enzyme Function | FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has beta-xylosidase activity via its capacity to hydrolyze glycosidic linkages of beta-1,4-xylo-oligosaccharides of various lengths (X2 to X6), releasing xylose monomers. To a much lesser extent, also has alpha-L-arabinofuranosidase activity. Does not possess beta-D-glucosidase activity. Acts synergistically with Xyn10D-Fae1A to increase the release of xylose from xylan. {ECO:0000269|PubMed:19304844}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:19304844}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19304844}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Mutagenesis (5); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Hydrolase;Polysaccharide degradation;Reference proteome;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| 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 | 96,224 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for pNP-beta-D-xylopyranoside (pNPX) (at 37 degrees Celsius and pH 5.0) {ECO:0000269|PubMed:19304844}; Note=kcat is 9.7 sec(-1) for the beta-xylosidase activity with pNPX as substrate (at 37 degrees Celsius and pH 5.0).; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.37; |