| IED ID | IndEnz0011000358 |
| Enzyme Type ID | glucanase000358 |
| Protein Name |
Endoglucanase EC 3.2.1.4 Cellulase Endo-1,4-beta-glucanase |
| Gene Name | |
| Organism | Cellulomonas uda |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Cellulomonadaceae Cellulomonas Cellulomonas uda |
| Enzyme Sequence | MPLRALVAVIVTTAVMLVPRAWAQTAWERYKARFMMPDARIIDTANGNVSHTEGQGFAMLLAVANNDRPAFDKLWQWTDSTLRDKSNGLFYWRYNPVAPDPIADKNNATDGDTLIAWALLRAQKQWQDKRYATASDAITASLLKYTVVTFAGRQVMLPGVKGFNRNDHLNLNPSYFIFPAWRAFAERTHLTAWRTLQSDGQALLGQMGWGKSHLPSDWVALRADGKMLPAKEWPPRMSFDAIRIPLYISWVDPHSALLAPWKAWMQSYPRLQTPAWINVSTNEVAPWNMAGGLLAVRDLTLGEPLERRRLTTRMIITPPASSCWSGWRNRISASAVMALQVSQPVCLRAERKEQERLTM |
| Enzyme Length | 359 |
| Uniprot Accession Number | P18336 |
| Absorption | |
| Active Site | ACT_SITE 53; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 110; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10058 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; |
| DNA Binding | |
| EC Number | 3.2.1.4 |
| Enzyme Function | 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); Chain (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|Ref.1 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,690 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |