| IED ID | IndEnz0008000333 |
| Enzyme Type ID | cellulase000333 |
| Protein Name |
Endoglucanase EC 3.2.1.4 Cellulase Endo-1,4-beta-glucanase |
| Gene Name | eglA |
| Organism | Clostridium saccharobutylicum |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium saccharobutylicum |
| Enzyme Sequence | MFSKIKKINFFKKTFSFLIAVVMMLFTVLGTNTYKAEAATTSFGGQLKVVGSQLCDSNGKPIQLKGMSSHGLQWYVNFVNYDSMKFLRDKWGVNVIRAAMYTNEGGYISNPSSQKEKIKKIVQDAIDLNMYVIIDWHILSDNNPNTYKEQAKSFFQEMAEEYGKYSNVIYEICNEPNGGTNWANDIKPYANYIIPAIRAIDPNNIIIVGTSTWSQDVDIAADNPLRYSNIMYTCHFYAGTHTQSLRDKINYAMSKGIAIFVTEWGTSDASGNGGPYLDESQKWVDFMASKNISWTNWALCDKSEASAALKSGSSTTGGWTDSDLTTSGLFVKKSIGGSNTTSQTSAPTFSLQSGTYDSAQTVTLTSSDNDSVIHYTTDGTTPTSSSPVYTSPITISKTTTVKAFTTKTGMTDSNITSAVYTISNTDPVKQVSAPTFSYNQEHTIQLKL |
| Enzyme Length | 448 |
| Uniprot Accession Number | P15704 |
| Absorption | |
| Active Site | ACT_SITE 175; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 263; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O85465 |
| Activity Regulation | |
| Binding Site | BINDING 70; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 101; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 137; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 237; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 297; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465 |
| 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 | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Region (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..34 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,366 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |