| IED ID | IndEnz0008000383 |
| Enzyme Type ID | cellulase000383 |
| Protein Name |
1,4-beta-D-glucan cellobiohydrolase B EC 3.2.1.91 Beta-glucancellobiohydrolase B Exocellobiohydrolase B Exoglucanase B |
| Gene Name | cbhB |
| 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 | MSSFQIYRAALLLSILATANAQQVGTYTTETHPSLTWQTCTSDGSCTTNDGEVVIDANWRWVHSTSSATNCYTGNEWDTSICTDDVTCAANCALDGATYEATYGVTTSGSELRLNFVTQGSSKNIGSRLYLMSDDSNYELFKLLGQEFTFDVDVSNLPCGLNGALYFVAMDADGGTSEYSGNKAGAKYGTGYCDSQCPRDLKFINGEANCDGWEPSSNNVNTGVGDHGSCCAEMDVWEANSISNAFTAHPCDSVSQTMCDGDSCGGTYSASGDRYSGTCDPDGCDYNPYRLGNTDFYGPGLTVDTNSPFTVVTQFITDDGTSSGTLTEIKRLYVQNGEVIANGASTYSSVNGSSITSAFCESEKTLFGDENVFDKHGGLEGMGEAMAKGMVLVLSLWDDYAADMLWLDSDYPVNSSASTPGVARGTCSTDSGVPATVEAESPNAYVTYSNIKFGPIGSTYSSGSSSGSGSSSSSSSTTTKATSTTLKTTSTTSSGSSSTSAAQAYGQCGGQGWTGPTTCVSGYTCTYENAYYSQCL |
| Enzyme Length | 536 |
| Uniprot Accession Number | Q9UVS8 |
| Absorption | |
| Active Site | ACT_SITE 233; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 238; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; |
| DNA Binding | |
| EC Number | 3.2.1.91 |
| Enzyme Function | FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. {ECO:0000250, ECO:0000269|PubMed:15182839}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Region (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Disulfide bond;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:10508057, ECO:0000269|PubMed:15182839}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,219 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.91; |