Detail Information for IndEnz0008000066
IED ID IndEnz0008000066
Enzyme Type ID cellulase000066
Protein Name Endoglucanase
EC 3.2.1.4
Cellulase
Endo-1,4-beta-glucanase
Gene Name bglC gld
Organism Bacillus subtilis
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis
Enzyme Sequence MKRSISIFITCLLIAVLTMGGLLPSPASAAGTKTPVAKNGQLSIKGTQLVNRDGKAVQLKGISSHGLQWYGDFVNKDSLKWLRDDWGITVFRAAMYTADGGYIDNPSVKNKVKEAVEAAKELGIYVIIDWHILNDGNPNQNKEKAKEFFKEMSSLYGNTPNVIYEIANEPNGDVNWKRDIKPYAEEVISVIRKNDPDNIIIVGTGTWSQDVNDAADDQLKDANVMYALHFYAGTHGQSLRDKANYALSKGAPIFVTEWGTSDASGNGGVFLDQSREWLNYLDSKNISWVNWNLSDKQESSSALKPGASKTGGWPLTDLTASGTFVRENIRGTKDSTKDVPETPAQDNPTQEKGVSVQYKAGDGRVNSNQIRPQLHIKNNGNATVDLKDVTARYWYNVKNKGQNFDCDYAQMGCGNLTHKFVTLHKPKQGADTYLELGFKTGTLSPGASTGNIQLRLHNDDWSNYAQSGDYSFFQSNTFKTTKKITLYHQGKLIWGTEPN
Enzyme Length 499
Uniprot Accession Number P07983
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); Binding site (5); Chain (1); Domain (1); Erroneous initiation (1); Region (4); Signal peptide (1)
Keywords Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..29
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 55,187
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda