IED ID | IndEnz0008000022 |
Enzyme Type ID | cellulase000022 |
Protein Name |
Endoglucanase E1 EC 3.2.1.4 Cellulase E1 Endo-1,4-beta-glucanase E1 Endocellulase E1 |
Gene Name | Acel_0614 |
Organism | Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Acidothermales Acidothermaceae Acidothermus Acidothermus cellulolyticus Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) |
Enzyme Sequence | MPRALRRVPGSRVMLRVGVVVAVLALVAALANLAVPRPARAAGGGYWHTSGREILDANNVPVRIAGINWFGFETCNYVVHGLWSRDYRSMLDQIKSLGYNTIRLPYSDDILKPGTMPNSINFYQMNQDLQGLTSLQVMDKIVAYAGQIGLRIILDRHRPDCSGQSALWYTSSVSEATWISDLQALAQRYKGNPTVVGFDLHNEPHDPACWGCGDPSIDWRLAAERAGNAVLSVNPNLLIFVEGVQSYNGDSYWWGGNLQGAGQYPVVLNVPNRLVYSAHDYATSVYPQTWFSDPTFPNNMPGIWNKNWGYLFNQNIAPVWLGEFGTTLQSTTDQTWLKTLVQYLRPTAQYGADSFQWTFWSWNPDSGDTGGILKDDWQTVDTVKDGYLAPIKSSIFDPVGASASPSSQPSPSVSPSPSPSPSASRTPTPTPTPTASPTPTLTPTATPTPTASPTPSPTAASGARCTASYQVNSDWGNGFTVTVAVTNSGSVATKTWTVSWTFGGNQTITNSWNAAVTQNGQSVTARNMSYNNVIQPGQNTTFGFQASYTGSNAAPTVACAAS |
Enzyme Length | 562 |
Uniprot Accession Number | P54583 |
Absorption | |
Active Site | ACT_SITE 203; /note=Proton donor; ACT_SITE 323; /note=Nucleophile |
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: Has a very high specific activity on carboxymethylcellulose. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 81 degrees Celsius. Thermostable.; |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (17); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Helix (12); Region (2); Signal peptide (1); Turn (9) |
Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..41 |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 1ECE; 1VRX; |
Mapped Pubmed ID | 15917594; |
Motif | |
Gene Encoded By | |
Mass | 60,748 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |