IED ID | IndEnz0011000118 |
Enzyme Type ID | glucanase000118 |
Protein Name |
Endoglucanase 5A EC 3.2.1.4 Alkaline cellulase Endo-1,4-beta-glucanase 5A |
Gene Name | cel5A |
Organism | Salipaludibacillus agaradhaerens (Bacillus agaradhaerens) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Salipaludibacillus Salipaludibacillus agaradhaerens (Bacillus agaradhaerens) |
Enzyme Sequence | MKKITTIFVVLLMTVALFSIGNTTAADNDSVVEEHGQLSISNGELVNERGEQVQLKGMSSHGLQWYGQFVNYESMKWLRDDWGINVFRAAMYTSSGGYIDDPSVKEKVKEAVEAAIDLDIYVIIDWHILSDNDPNIYKEEAKDFFDEMSELYGDYPNVIYEIANEPNGSDVTWGNQIKPYAEEVIPIIRNNDPNNIIIVGTGTWSQDVHHAADNQLADPNVMYAFHFYAGTHGQNLRDQVDYALDQGAAIFVSEWGTSAATGDGGVFLDEAQVWIDFMDERNLSWANWSLTHKDESSAALMPGANPTGGWTEAELSPSGTFVREKIRESASIPPSDPTPPSDPGEPDPTPPSDPGEYPAWDPNQIYTNEIVYHNGQLWQAKWWTQNQEPGDPYGPWEPLN |
Enzyme Length | 400 |
Uniprot Accession Number | O85465 |
Absorption | |
Active Site | ACT_SITE 165; /note="Proton donor"; /evidence="ECO:0000305|PubMed:12595701, ECO:0000305|PubMed:9485319, ECO:0000305|PubMed:9718293, ECO:0000305|Ref.4"; ACT_SITE 254; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0000269|Ref.4, ECO:0007744|PDB:1H11, ECO:0007744|PDB:1QI2, ECO:0007744|PDB:5A3H, ECO:0007744|PDB:6A3H, ECO:0007744|PDB:8A3H" |
Activity Regulation | |
Binding Site | BINDING 61; /note="Substrate"; /evidence="ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H"; BINDING 92; /note="Substrate"; /evidence="ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0, ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H"; BINDING 127; /note="Substrate"; /evidence="ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9718293, ECO:0000269|Ref.4, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:3A3H"; BINDING 228; /note="Substrate"; /evidence="ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:3A3H"; BINDING 288; /note="Substrate"; /evidence="ECO:0000269|PubMed:12595701, ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293, ECO:0000269|Ref.4, ECO:0007744|PDB:1H5V, ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0, ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H, ECO:0007744|PDB:8A3H" |
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; Evidence={ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293}; |
DNA Binding | |
EC Number | 3.2.1.4 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (13); Binding site (5); Chain (1); Compositional bias (1); Domain (1); Helix (13); Region (4); Signal peptide (1); Turn (4) |
Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:9485319 |
Structure 3D | X-ray crystallography (20) |
Cross Reference PDB | 1A3H; 1E5J; 1H11; 1H2J; 1H5V; 1HF6; 1OCQ; 1QHZ; 1QI0; 1QI2; 1W3K; 1W3L; 2A3H; 2V38; 3A3H; 4A3H; 5A3H; 6A3H; 7A3H; 8A3H; |
Mapped Pubmed ID | 10731432; 11679762; 11828460; 12812472; 15356002; |
Motif | |
Gene Encoded By | |
Mass | 44,702 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |