| IED ID | IndEnz0008000049 |
| Enzyme Type ID | cellulase000049 |
| Protein Name |
1,4-beta-D-glucan cellobiohydrolase CEL6A EC 3.2.1.91 Beta-glucancellobiohydrolase CEL6A Exocellobiohydrolase CEL6A Exoglucanase CEL6A |
| Gene Name | cel6A MGG_05520 |
| Organism | Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Pyriculariaceae Pyricularia Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae) Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) |
| Enzyme Sequence | MASKLFLAAALLQGALSSPLAVEERQACAAQWGQCGGQDYTGPTCCQSGSTCVVSNQWYSQCLPGSSNPTTTSRTSTSSSSSTSRTSSSTSRPPSSVPTTPTSVPPTITTTPTTTPTGGSGPGTTASFTGNPFAGVNLFPNKFYSSEVHTLAIPSLTGSLVAKASAVAQVPSFQWLDIAAKVETLMPGALADVRAANAAGGNYAAQLVVYDLPDRDCAAAASNGEFSIADGGVVKYKAYIDAIRKQLLAYSDVRTILVIEPDSLANMVTNMGVPKCAGAKDAYLECTIYAVKQLNLPHVAMYLDGGHAGWLGWPANLQPAADLFGKLYADAGKPSQLRGMATNVANYNAWDLTTAPSYTTPNPNFDEKKYISAFAPLLAAKGWSAHFIIDQGRSGKQPTGQKEWGHWCNQQGVGFGRRPSANTGSELADAFVWIKPGGECDGVSDPTAPRFDHFCGTDYGAMSDAPQAGQWFQKYFEMLLTNANPPL |
| Enzyme Length | 487 |
| Uniprot Accession Number | G4MM92 |
| Absorption | |
| Active Site | ACT_SITE 216; /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"; ACT_SITE 262; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"; ACT_SITE 441; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q9C1S9, ECO:0000255|PROSITE-ProRule:PRU10056" |
| Activity Regulation | |
| Binding Site | BINDING 175; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 177; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 307; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 310; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 346; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 407; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 435; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 439; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9 |
| 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:20709852}; |
| DNA Binding | |
| EC Number | 3.2.1.91 |
| Enzyme Function | FUNCTION: Exoglucanase that plays an important function in biomass degradation by catalyzing the hydrolysis of the non-reducing end beta-1,4-glucosidic linkages in cellulose and cellotetraose to release cellobiose. Shows higher hydrolytic activities on phosphoric acid-swollen cellulose (PSC), beta-glucan, and cellooligosaccharide derivatives than on cellulose, of which the best substrates were cellooligosaccharides. {ECO:0000269|PubMed:20709852}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-50 degrees Celsius. {ECO:0000269|PubMed:20709852}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-9.0. {ECO:0000269|PubMed:20709852}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (8); Chain (1); Disulfide bond (2); Domain (1); Region (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression increases during infection of rice. {ECO:0000269|PubMed:20709852}. |
| 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 | 51,225 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24.3 mM for cellotetraose {ECO:0000269|PubMed:20709852}; Vmax=454.5 umol/min/mg enzyme toward cellotetraose {ECO:0000269|PubMed:20709852}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |