Detail Information for IndEnz0011000235
IED ID IndEnz0011000235
Enzyme Type ID glucanase000235
Protein Name Endoglucanase
EC 3.2.1.4
Carboxymethyl-cellulase
CMCase
Cellulase
Endo-1,4-beta-glucanase
Gene Name eglS bglC gld BSU18130
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MKRSISIFITCLLITLLTMGGMIASPASAAGTKTPVAKNGQLSIKGTQLVNRDGKAVQLKGISSHGLQWYGEYVNKDSLKWLRDDWGITVFRAAMYTADGGYIDNPSVKNKVKEAVEAAKELGIYVIIDWHILNDGNPNQNKEKAKEFFKEMSSLYGNTPNVIYEIANEPNGDVNWKRDIKPYAEEVISVIRKNDPDNIIIVGTGTWSQDVNDAADDQLKDANVMYALHFYAGTHGQFLRDKANYALSKGAPIFVTEWGTSDASGNGGVFLDQSREWLKYLDSKTISWVNWNLSDKQESSSALKPGASKTGGWRLSDLSASGTFVRENILGTKDSTKDIPETPSKDKPTQENGISVQYRAGDGSMNSNQIRPQLQIKNNGNTTVDLKDVTARYWYKAKNKGQNFDCDYAQIGCGNVTHKFVTLHKPKQGADTYLELGFKNGTLAPGASTGNIQLRLHNDDWSNYAQSGDYSFFKSNTFKTTKKITLYDQGKLIWGTEPN
Enzyme Length 499
Uniprot Accession Number P10475
Absorption
Active Site ACT_SITE 169; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O85465; ACT_SITE 257; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O85465
Activity Regulation
Binding Site BINDING 65; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 96; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 131; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 231; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O85465; BINDING 291; /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); Beta strand (23); Binding site (5); Chain (1); Domain (1); Erroneous initiation (1); Helix (17); Region (3); Sequence conflict (1); Signal peptide (1); Turn (4)
Keywords 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..29; /evidence=ECO:0000269|PubMed:7710279
Structure 3D X-ray crystallography (5); NMR spectroscopy (1)
Cross Reference PDB 2L8A; 3PZT; 3PZU; 3PZV; 6UFV; 6UFW;
Mapped Pubmed ID 21880019;
Motif
Gene Encoded By
Mass 55,287
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.4;