| IED ID | IndEnz0011000357 | 
| Enzyme Type ID | glucanase000357 | 
| Protein Name | 
                        
                            
                                Endoglucanase  EC 3.2.1.4 Cellulase Endo-1,4-beta-glucanase Endo-K  | 
                    
| Gene Name | |
| Organism | Bacillus sp. (strain KSM-330) | 
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain KSM-330) | 
| Enzyme Sequence | MVEKRKIFTVLCACGIGFTSYTSCISAAAIDNDTLINNGHKINSSIITNSSQVSAVAKEMKPFPQQVNYSGILKPNHVSQESLNNAVKNYYNDWKKKYLKNDLSSLPGGYYVKGEITGNPDGFRPLGTSEGQGYGMIITVLMAGHDSNAQTIYDGLFKTARAFKSSINPNLMGWVVADDKKAQGHFDSATDGDLDIAYSLLLAHKQWGSSGKINYLKEAQNMITKGIKASNVTKNNGLNLGDWGDKSTFDTRPSDWMMSHLRAFYEFTGDKTWLNVIDNLYNTYTNFTNKYSPKTGLISDFVVKNPPQPAPKDFLDESKYTDSYYYNASRVPLRIVMDYAMYGEKRGKVISDKVATWIKSKTKGNPSKIVDGYKLDGTNIGDYPTAVYVSPFIAAGTTNSKNQEWVNSGWDWMKNKKESYFSDSYNLLTMLFLTGNWWKPIPDEKKIQSPINLEVQSELKEQD | 
| Enzyme Length | 463 | 
| Uniprot Accession Number | P29019 | 
| Absorption | |
| Active Site | ACT_SITE 130; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 191; /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 | |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.2. Active from pH 4.5 to 6.5.; | 
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Propeptide (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 | PTM: The N- and the C-terminus may be subjected to proteolysis. | 
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 51,883 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |