| IED ID | IndEnz0008000354 |
| Enzyme Type ID | cellulase000354 |
| Protein Name |
Exoglucanase 1 EC 3.2.1.91 1,4-beta-cellobiohydrolase Cellobiohydrolase 7A Cel7A Exocellobiohydrolase I CBHI Exoglucanase I |
| Gene Name | cbh1 M419DRAFT_125125 |
| Organism | Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) |
| Enzyme Sequence | MYRKLAVISAFLATARAQSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNCYDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSAQKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMDADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDNRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAINRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLTQFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTSSGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSGGNPPGGNPPGTTTTRRPATTTGSSPGPTQSHYGQCGGIGYSGPTVCASGTTCQVLNPYYSQCL |
| Enzyme Length | 514 |
| Uniprot Accession Number | A0A024RXP8 |
| Absorption | |
| Active Site | ACT_SITE 229; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P62694; ACT_SITE 234; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P62694 |
| 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:0000250|UniProtKB:P62694}; |
| 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. 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. {ECO:0000250|UniProtKB:P62694}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (12); Domain (1); Glycosylation (15); Modified residue (1); Region (3); Signal peptide (1); Site (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P62694}. |
| Modified Residue | MOD_RES 18; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P62694 |
| Post Translational Modification | PTM: N-glycosylated. A high mannose glycan is attached to Asn-287 (predominantly Man(8)GlcNAc(2)) and single GlcNAc occupancy is observed at Asn-62 and Asn-401 with some site heterogeneity depending on strains and fermentation conditions. {ECO:0000269|PubMed:11270873}.; 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. O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose. {ECO:0000250|UniProtKB:P62694}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,111 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.91; |