| IED ID | IndEnz0011000288 |
| Enzyme Type ID | glucanase000288 |
| Protein Name |
Endoglucanase E-2 EC 3.2.1.4 Cellulase E-2 Cellulase E2 Endo-1,4-beta-glucanase E-2 |
| Gene Name | celB |
| Organism | Thermobifida fusca (Thermomonospora fusca) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Nocardiopsaceae Thermobifida Thermobifida fusca (Thermomonospora fusca) |
| Enzyme Sequence | MSPRPLRALLGAAAAALVSAAALAFPSQAAANDSPFYVNPNMSSAEWVRNNPNDPRTPVIRDRIASVPQGTWFAHHNPGQITGQVDALMSAAQAAGKIPILVVYNAPGRDCGNHSSGGAPSHSAYRSWIDEFAAGLKNRPAYIIVEPDLISLMSSCMQHVQQEVLETMAYAGKALKAGSSQARIYFDAGHSAWHSPAQMASWLQQADISNSAHGIATNTSNYRWTADEVAYAKAVLSAIGNPSLRAVIDTSRNGNGPAGNEWCDPSGRAIGTPSTTNTGDPMIDAFLWIKLPGEADGCIAGAGQFVPQAAYEMAIAAGGTNPNPNPNPTPTPTPTPTPPPGSSGACTATYTIANEWNDGFQATVTVTANQNITGWTVTWTFTDGQTITNAWNADVSTSGSSVTARNVGHNGTLSQGASTEFGFVGSKGNSNSVPTLTCAAS |
| Enzyme Length | 441 |
| Uniprot Accession Number | P26222 |
| Absorption | |
| Active Site | ACT_SITE 110; ACT_SITE 148; /note=Proton donor; ACT_SITE 296; /note=Nucleophile |
| Activity Regulation | |
| Binding Site | |
| 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 | PATHWAY: Glycan metabolism; cellulose degradation. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (14); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Helix (10); Mutagenesis (1); Region (3); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. |
| Signal Peptide | SIGNAL 1..31; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|Ref.3" |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1TML; 2BOD; 2BOE; 2BOF; 2BOG; 3RPT; |
| Mapped Pubmed ID | 16185060; 22021856; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,844 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |