| IED ID | IndEnz0008000042 |
| Enzyme Type ID | cellulase000042 |
| Protein Name |
Exoglucanase/xylanase Includes: Exoglucanase EC 3.2.1.91 1,4-beta-cellobiohydrolase Beta-1,4-glycanase CEX Exocellobiohydrolase ; Endo-1,4-beta-xylanase B Xylanase B EC 3.2.1.8 |
| Gene Name | cex xynB |
| Organism | Cellulomonas fimi |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Cellulomonadaceae Cellulomonas Cellulomonas fimi |
| Enzyme Sequence | MPRTTPAPGHPARGARTALRTTRRRAATLVVGATVVLPAQAATTLKEAADGAGRDFGFALDPNRLSEAQYKAIADSEFNLVVAENAMKWDATEPSQNSFSFGAGDRVASYAADTGKELYGHTLVWHSQLPDWAKNLNGSAFESAMVNHVTKVADHFEGKVASWDVVNEAFADGDGPPQDSAFQQKLGNGYIETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDCVGFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQAADYKKVVQACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYAKKPAYAAVMEAFGASPTPTPTTPTPTPTTPTPTPTSGPAGCQVLWGVNQWNTGFTANVTVKNTSSAPVDGWTLTFSFPSGQQVTQAWSSTVTQSGSAVTVRNAPWNGSIPAGGTAQFGFNGSHTGTNAAPTAFSLNGTPCTVG |
| Enzyme Length | 484 |
| Uniprot Accession Number | P07986 |
| Absorption | |
| Active Site | ACT_SITE 168; /note="Proton donor"; /evidence="ECO:0000269|PubMed:7918478"; ACT_SITE 274; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10061, ECO:0000269|PubMed:1678739" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; |
| DNA Binding | |
| EC Number | 3.2.1.91; 3.2.1.8 |
| Enzyme Function | FUNCTION: Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity.; FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (24); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (2); Helix (16); Mutagenesis (1); Region (2); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Repeat;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..41 |
| Structure 3D | NMR spectroscopy (2); X-ray crystallography (15) |
| Cross Reference PDB | 1EXG; 1EXH; 1EXP; 1FH7; 1FH8; 1FH9; 1FHD; 1J01; 2EXO; 2HIS; 2XYL; 3CUF; 3CUG; 3CUH; 3CUI; 3CUJ; 6QFS; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,291 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.91; |