IED ID | IndEnz0008000328 |
Enzyme Type ID | cellulase000328 |
Protein Name |
Endoglucanase EC 3.2.1.4 Alkaline cellulase Endo-1,4-beta-glucanase |
Gene Name | |
Organism | Alkalihalobacillus akibai (strain ATCC 43226 / DSM 21942 / CIP 109018 / JCM 9157 / 1139) (Bacillus akibai) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Alkalihalobacillus Alkalihalobacillus akibai Alkalihalobacillus akibai (strain ATCC 43226 / DSM 21942 / CIP 109018 / JCM 9157 / 1139) (Bacillus akibai) |
Enzyme Sequence | MMLRKKTKQLISSILILVLLLSLFPTALAAEGNTREDNFKHLLGNDNVKRPSEAGALQLQEVDGQMTLVDQHGEKIQLRGMSTHGLQWFPEILNDNAYKALANDWESNMIRLAMYVGENGYASNPELIKSRVIKGIDLAIENDMYVIVDWHVHAPGDPRDPVYAGAEDFFRDIAALYPNNPHIIYELANEPSSNNNGGAGIPNNEEGWNAVKEYADPIVEMLRDSGNADDNIIIVGSPNWSQRPDLAADNPIDDHHTMYTVHFYTGSHAASTESYPPETPNSERGNVMSNTRYALENGVAVFATEWGTSQANGDGGPYFDEADVWIEFLNENNISWANWSLTNKNEVSGAFTPFELGKSNATSLDPGPDQVWVPEELSLSGEYVRARIKGVNYEPIDRTKYTKVLWDFNDGTKQGFGVNGDSPVEDVVIENEAGALKLSGLDASNDVSEGNYWANARLSADGWGKSVDILGAEKLTMDVIVDEPTTVSIAAIPQGPSANWVNPNRAIKVEPTNFVPLEDKFKAELTITSADSPSLEAIAMHAENNNINNIILFVGTEGADVIYLDNIKVIGTEVEIPVVHDPKGEAVLPSVFEDGTRQGWDWAGESGVKTALTIEEANGSNALSWEFGYPEVKPSDNWATAPRLDFWKSDLVRGENDYVTFDFYLDPVRATEGAMNINLVFQPPTNGYWVQAPKTYTINFDELEEPNQVNGLYHYEVKINVRDITNIQDDTLLRNMMIIFADVESDFAGRVFVDNVRFEGAATTEPVEPEPVDPGEETPPVDEKEAKTEQKEAEKEEKEE |
Enzyme Length | 800 |
Uniprot Accession Number | P06564 |
Absorption | |
Active Site | ACT_SITE 190; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 305; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O85465 |
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 9.0.; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (12); Chain (1); Compositional bias (1); Helix (2); Region (1); Signal peptide (1); Turn (1) |
Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1UWW; |
Mapped Pubmed ID | 15136030; |
Motif | |
Gene Encoded By | |
Mass | 88,602 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |