| IED ID | IndEnz0008000038 |
| Enzyme Type ID | cellulase000038 |
| Protein Name |
Exoglucanase-6A EC 3.2.1.91 1,4-beta-cellobiohydrolase 6A Avicelase 2 Beta-glucancellobiohydrolase 6A Exocellobiohydrolase 6A |
| Gene Name | cel6A avi2 |
| Organism | Humicola insolens (Soft-rot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Humicola Humicola insolens (Soft-rot fungus) |
| Enzyme Sequence | MAKFFLTAAFAAAALAAPVVEERQNCAPTWGQCGGIGFNGPTCCQSGSTCVKQNDWYSQCLPGSQVTTTSTTSTSSSSTTSRATSTTRTGGVTSITTAPTRTVTIPGGATTTASYNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVETLSEIRAANQAGANPPYAAQIVVYDLPDRDCAAAASNGEWAIANNGANNYKGYINRIREILISFSDVRTILVIEPDSLANMVTNMNVAKCSGAASTYRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSISSPPPYTSPNPNYDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTSDTTAARYDYHCGLEDALKPAPEAGQWFQAYFEQLLRNANPPF |
| Enzyme Length | 476 |
| Uniprot Accession Number | Q9C1S9 |
| Absorption | |
| Active Site | ACT_SITE 252; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10057, ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12842048"; ACT_SITE 431; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10056, ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048" |
| Activity Regulation | |
| Binding Site | BINDING 163; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"; BINDING 165; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"; BINDING 297; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"; BINDING 300; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"; BINDING 336; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"; BINDING 397; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"; BINDING 425; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048"; BINDING 429; /note="Substrate"; /evidence="ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048" |
| 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|PubMed:9335167}; |
| DNA Binding | |
| EC Number | 3.2.1.91 |
| Enzyme Function | FUNCTION: Plays a central role in the recycling of plant biomass. 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:0000269|PubMed:9882628}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Binding site (8); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Helix (14); Region (3); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (11) |
| Cross Reference PDB | 1BVW; 1GZ1; 1OC5; 1OC6; 1OC7; 1OCB; 1OCJ; 1OCN; 2BVW; 4I5R; 4I5U; |
| Mapped Pubmed ID | 12744312; 23404363; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,276 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.91; |