Detail Information for IndEnz0011000354
IED ID IndEnz0011000354
Enzyme Type ID glucanase000354
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