| IED ID | IndEnz0011000378 |
| Enzyme Type ID | glucanase000378 |
| Protein Name |
Endo-beta-1,4-glucanase B Endoglucanase B EC 3.2.1.4 Carboxymethylcellulase B Cellulase B |
| Gene Name | eglB eng1 |
| Organism | Aspergillus niger |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger |
| Enzyme Sequence | MKFQSTLLLAAAAGSALAVPHGSGHKKRASVFEWFGSNESGAEFGTNIPGVWGTDYIFPDPSTISTLIGKGMNFFRVQFMMERLLPDSMTGSYDEEYLANLTTVVKAVTDGGAHALIDPHNYGRYNGEIISSTSDFQTFWQNLAGQYKDNDLVMFDTNNEYYDMDQDLVLNLNQAAINGIRAAGASQYIFVEGNSWTGAWTWVDVNDNMKNLTDPEDKIVYEMHQYLDSDGSGTSETCVSGTIGKERITDATQWLKDNKKVGFIGEYAGGSNDVCRSAVSGMLEYMANNTDVWKGASWWAAGPWWGDYIFSLEPPDGTAYTGMLDILETYL |
| Enzyme Length | 331 |
| Uniprot Accession Number | O74706 |
| Absorption | |
| Active Site | ACT_SITE 160; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 266; /note=Nucleophile; /evidence=ECO:0000250 |
| 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 | FUNCTION: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates. {ECO:0000269|PubMed:16233124}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:16233124}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:16233124}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (10); Chain (1); Glycosylation (4); Helix (11); Sequence conflict (12); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is under the control of the xylanolytic transcriptional activator xlnR. {ECO:0000269|PubMed:9758775}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 5I77; 5I78; 5I79; |
| Mapped Pubmed ID | 27154222; |
| Motif | |
| Gene Encoded By | |
| Mass | 36,559 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.4; |