Detail Information for IndEnz0011000111
IED ID IndEnz0011000111
Enzyme Type ID glucanase000111
Protein Name Endoglucanase B
EC 3.2.1.4
Cellulase B
Endo-1,4-beta-glucanase B
Gene Name celB
Organism Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) (Bacillus cellulosilyticus)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Evansella Evansella cellulosilytica Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) (Bacillus cellulosilyticus)
Enzyme Sequence MKKITTIFVVLLMTLALFIIGNTTAADDYSVVEEHGQLSISNGELVNDRGEPVQLKGMSSHGLQWYGQFVNYESMKWLRDDWGITVFRAAMYTSSGGYIEDPSVKEKVKEAVEAAIDLGIYVIIDWHILSDNDPNIYKEEAKDFFDEMSELYGDYPNVIYEIANEPNGSDVTWDNQIKPYAEEVIPVIRNNDPNNIIIVGTGTWSQDVHHAADNQLTDPNVMYAFHFYAGTHGQNLRDQVDYALDQGAAIFVSEWGTSEATGDGGVFLDEAQVWIDFMDERNLSWANWSLTHKDESSAALMPGASPTGGWTEAELSPSGTFVREKIRESATTPPSDPTPPSDPDPGEPEPDPGEPDPTPPSDPGDYPAWDPNTIYTDEIVYHNGQLWQAKWWTQNQEPGDPYGPWEPLN
Enzyme Length 409
Uniprot Accession Number P06565
Absorption
Active Site ACT_SITE 165; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 254; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O85465
Activity Regulation
Binding Site BINDING 61; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 92; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 127; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 228; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 288; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465
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
Pathway
nucleotide Binding
Features Active site (2); Binding site (5); Chain (1); Compositional bias (1); Region (4)
Keywords Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,690
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda