IED ID | IndEnz0004000045 |
Enzyme Type ID | xylanase000045 |
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 (15); Region (3); Sequence conflict (1); Signal peptide (1); Turn (5) |
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 | NMR spectroscopy (1); X-ray crystallography (5) |
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; |