| IED ID | IndEnz0008000015 |
| Enzyme Type ID | cellulase000015 |
| 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 |