| IED ID | IndEnz0011000301 | 
| Enzyme Type ID | glucanase000301 | 
| Protein Name | 
                        
                            
                                Endoglucanase A  EC 3.2.1.4 Cellulase A Endo-1,4-beta-glucanase A  | 
                    
| Gene Name | cenA | 
| 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 | MSTRRTAAALLAAAAVAVGGLTALTTTAAQAAPGCRVDYAVTNQWPGGFGANVTITNLGDPVSSWKLDWTYTAGQRIQQLWNGTASTNGGQVSVTSLPWNGSIPTGGTASFGFNGSWAGSNPTPASFSLNGTTCTGTVPTTSPTPTPTPTTPTPTPTPTPTPTPTVTPQPTSGFYVDPTTQGYRAWQAASGTDKALLEKIALTPQAYWVGNWADASHAQAEVADYTGRAVAAGKTPMLVVYAIPGRDCGSHSGGGVSESEYARWVDTVAQGIKGNPIVILEPDALAQLGDCSGQGDRVGFLKYAAKSLTLKGARVYIDAGHAKWLSVDTPVNRLNQVGFEYAVGFALNTSNYQTTADSKAYGQQISQRLGGKKFVIDTSRNGNGSNGEWCNPRGRALGERPVAVNDGSGLDALLWVKLPGESDGACNGGPAAGQWWQEIALEMARNARW | 
| Enzyme Length | 449 | 
| Uniprot Accession Number | P07984 | 
| Absorption | |
| Active Site | ACT_SITE 247; /evidence=ECO:0000255|PROSITE-ProRule:PRU10056; ACT_SITE 283; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10057; ACT_SITE 423; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10056 | 
| 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 (3); Chain (1); Compositional bias (2); Disulfide bond (3); Domain (1); Region (3); Signal peptide (1) | 
| Keywords | Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Signal | 
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The linker region (also termed 'hinge') may be a potential site for proteolysis.; PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. | 
| Signal Peptide | SIGNAL 1..31; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 46,731 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |