IED ID | IndEnz0008000371 |
Enzyme Type ID | cellulase000371 |
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; |