| IED ID | IndEnz0008000167 |
| Enzyme Type ID | cellulase000167 |
| Protein Name |
Probable 1,4-beta-D-glucan cellobiohydrolase A EC 3.2.1.91 Beta-glucancellobiohydrolase A Cellobiohydrolase D Exocellobiohydrolase A Exoglucanase A |
| Gene Name | cbhA celD ACLA_088870 |
| Organism | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
| Enzyme Sequence | MYQRALLFSALATAVSAQQVGTQKAEVHPALTWQKCTAAGSCTDQKGSVVIDANWRWLHSTEDTTNCYTGNEWNAELCPDNEACAKNCALDGADYSGTYGVTADGSSLKLNFVTSANVGSRLYLMEDDETYQMFNLLNNEFTFDVDVSNLPCGLNGALYFVSMDADGGLSKYPGNKAGAKYGTGYCDSQCPRDLKFINGEANVEGWKPSDNDKNAGVGGYGSCCPEMDIWEANSISTAYTPHPCDGMEQTRCDGNDCGGTYSSTRYAGTCDPDGCDFNSFRMGNESFYGPGGLVDTKSPITVVTQFVTAGGTDSGALKEIRRVYVQGGKVIGNSASNVAGVEGDSITSDFCTAQKKAFGDEDIFSKHGGLEGMGKALNKMALIVSIWDDHASSMMWLDSTYPVDADASTPGVARGTCEHGLGDPETVESQHPDASVTFSNIKFGPIGSTYKSV |
| Enzyme Length | 453 |
| Uniprot Accession Number | A1CE97 |
| Absorption | |
| Active Site | ACT_SITE 226; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 231; /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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Glycosylation (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,214 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |