| IED ID | IndEnz0008000208 |
| Enzyme Type ID | cellulase000208 |
| 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 AN5176 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MYQRALLFSALLSVSRAQQAGTAQEEVHPSLTWQRCEASGSCTEVAGSVVLDSNWRWTHSVDGYTNCYTGNEWDATLCPDNESCAQNCAVDGADYEATYGITSNGDSLTLKFVTGSNVGSRVYLMEDDETYQMFDLLNNEFTFDVDVSNLPCGLNGALYFTSMDADGGLSKYEGNTAGAKYGTGYCDSQCPRDIKFINGLGNVEGWEPSDSDANAGVGGMGTCCPEMDIWEANSISTAYTPHPCDSVEQTMCEGDSCGGTYSDDRYGGTCDPDGCDFNSYRMGNTSFYGPGAIIDTSSKFTVVTQFIADGGSLSEIKRFYVQNGEVIPNSESNISGVEGNSITSEFCTAQKTAFGDEDIFAQHGGLSAMGDAASAMVLILSIWDDHHSSMMWLDSSYPTDADPSQPGVARGTCEQGAGDPDVVESEHADASVTFSNIKFGPIGSTF |
| Enzyme Length | 446 |
| Uniprot Accession Number | Q5B2Q4 |
| 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, ECO:0000269|PubMed:16844780}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Glycosylation (3); Region (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Repressed by D-glucose. {ECO:0000269|PubMed:12409103}. |
| 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 | 47,638 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |