| IED ID | IndEnz0008000353 |
| Enzyme Type ID | cellulase000353 |
| Protein Name |
Exoglucanase 1 EC 3.2.1.91 1,4-beta-cellobiohydrolase Cellobiohydrolase 7A Cel7A Exocellobiohydrolase I CBHI Exoglucanase I |
| Gene Name | cbh1 |
| Organism | Hypocrea jecorina (Trichoderma reesei) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) |
| Enzyme Sequence | MYRKLAVISAFLATARAQSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNCYDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSAQKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMDADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDNRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAINRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLTQFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTSSGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSGGNPPGGNRGTTTTRRPATTTGSSPGPTQSHYGQCGGIGYSGPTVCASGTTCQVLNPYYSQCL |
| Enzyme Length | 513 |
| Uniprot Accession Number | P62694 |
| Absorption | |
| Active Site | ACT_SITE 229; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:24341799, ECO:0000305|PubMed:8036495"; ACT_SITE 234; /note="Proton donor/acceptor"; /evidence="ECO:0000269|PubMed:24341799, ECO:0000305|PubMed:8036495" |
| 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; Evidence={ECO:0000269|Ref.4}; |
| DNA Binding | |
| EC Number | 3.2.1.91 |
| Enzyme Function | FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (Ref.4). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable). {ECO:0000269|Ref.4, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (37); Chain (1); Disulfide bond (12); Domain (1); Glycosylation (15); Helix (10); Modified residue (1); Region (3); Sequence conflict (1); Signal peptide (1); Site (1); Turn (6) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.4}. |
| Modified Residue | MOD_RES 18; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:1EGN, ECO:0007744|PDB:1Q2B, ECO:0007744|PDB:1Q2E" |
| Post Translational Modification | PTM: N-glycosylated. The catalytic core domain comprises three N-linked glycans which each consist of a single N-acetylglucosamine residue. {ECO:0000269|PubMed:9746354}.; PTM: O-glycosylated. Within the linker domain, all 8 threonines are variably glycosylated with between at least one, and up to three, mannose residues per site. All serines in this domain are at least partially glycosylated with a single mannose residue (PubMed:9746354). O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose (Probable). {ECO:0000269|PubMed:9746354, ECO:0000305|PubMed:26307003}. |
| Signal Peptide | SIGNAL 1..17; /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4" |
| Structure 3D | NMR spectroscopy (15); X-ray crystallography (27) |
| Cross Reference PDB | 1AZ6; 1AZH; 1AZJ; 1AZK; 1CBH; 1CEL; 1DY4; 1EGN; 1Q2B; 1Q2E; 2CBH; 2CEL; 2MWJ; 2MWK; 2V3I; 2V3R; 3CEL; 4C4C; 4C4D; 4CEL; 4D5I; 4D5J; 4D5O; 4D5P; 4D5Q; 4D5V; 4P1H; 4P1J; 4UWT; 4V0Z; 5CEL; 5OA5; 5X34; 5X35; 5X36; 5X37; 5X38; 5X39; 5X3C; 6CEL; 6GRN; 7CEL; |
| Mapped Pubmed ID | 11114249; 11336632; 14568538; 25765184; 28494147; 28860192; 30255965; 8951380; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,073 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.176;3.2.1.4;3.2.1.91; |