| IED ID | IndEnz0008000567 |
| Enzyme Type ID | cellulase000567 |
| Protein Name |
Endo-1,4-beta-xylanase B Xylanase B EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase B |
| Gene Name | xynB |
| Organism | Neocallimastix patriciarum (Rumen fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Chytridiomycota Chytridiomycota incertae sedis Neocallimastigomycetes Neocallimastigales Neocallimastigaceae Neocallimastix Neocallimastix patriciarum (Rumen fungus) |
| Enzyme Sequence | MKFSSANKILFSGLVASANAYDLLKDYAGDLKIGVAANAMRFSNSNYVNAMKAFNMMVAENDCKLSGIQQQKGVYNFNGCDNHYNKAKELGMEFRGHCLIWHSYQPSWFQNADANTLKNAIVDHITKTLQHYEGKIKVWDVVNEAIDDNSNGNGWNMRRSFLYNKVPNFVDLAFQTARKVSPNTKLFYNDYNAEGVYAKAESIYNFVSDLKKRNIPIDGVGLQYHVGAKEQPSYNKINDLIGRYCKLGLEVHITELDVKLQGDQNGQSQAFSNALKACLANSCCKAFLVWGVGDNDSWLGANEQALLFNGSYQPKPVYNTLLNILKTSARPASSSAKTLPGNSKSKTLPGVNSKTLPGNKSKTLPGASKTLPGNKSKTLPGGNSNTLPGNKSKTLPGGNSKTLPGNKSRTLPGGNSKTLPGGKSRTLPGGNSKTLPGGKSKTLPGGNSKTLPGGKSKTLPGGNSKTLPGGSSKTLPGGKSKTLPGGNSKTLPGGSSKTLPGGKSKTLPGGSSKTLPGGKSKTLPGGNSKTLPGGNSKTLPGGSSKTLPGGKSKTLPGGNSKTLPGGSSKTLPGGKSKTLPGGNSKTLPGGNSKTLPGGKSKTLPGGNSKTLPGGSSKTLPGGKSKTLPGGSSKTLPGGKSKTLPGGNSKTLPGGNSKTLPGGSSKTLPGGKSKTLPGGSSKTLPGGKSKTLPGGNSKTLPGGKSKTLPGGNSKTLPGGKSKTLPGGNSKTLPGGKSKTLPGGNSKTLPGGSSKTLPGGKSKTLPGGNSKTLPGGKSKTLPGGNTKTLPGGACKPTTVTVTQKVTVTVTVESQPTQGGMNQGGGNCAAKWGQCGGNGFNGPTCCQNGSRCQFVNEWYSQCL |
| Enzyme Length | 860 |
| Uniprot Accession Number | Q02290 |
| Absorption | |
| Active Site | ACT_SITE 144; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 255; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Hydrolyzes both unsubstituted (oat spelts) and highly substituted (rye and wheat) forms of arabinoxylanslans. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (7); Region (2); Repeat (47); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 88,052 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |