| IED ID | IndEnz0008000030 |
| Enzyme Type ID | cellulase000030 |
| Protein Name |
1,4-beta-D-glucan cellobiohydrolase CEL6C EC 3.2.1.91 Beta-glucancellobiohydrolase CEL6C Exocellobiohydrolase CEL6C Exoglucanase CEL6C |
| Gene Name | CEL6C Pa_4_2420 PODANS_4_2420 |
| Organism | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Podosporaceae Podospora Podospora anserina (Pleurage anserina) Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
| Enzyme Sequence | MKITSSAAALALVASAVAAPSPTTQDKPTKRQAGCASAVSLNAQTNVFKQYTLHANNFYRKEIEELAIPNLSDPSLEAAARKVADTGSFVWLDTIANVDRLEPALAEVPCNEILGVVVYDLPGRDCAAKASNGELKVGELNRYKTEFIDRIASILKAHPNTAVALVIEPDSLPNLVTNSDVQACRNSAAGYRDGVAYALKTLNLPNVVQYIDAGHGGWLGWDANLKPGAEELAKAYKAAGSPKQFRGIATNVAGWNAWDLSPGEFSSASDAKYNSCQNERTYVNTFGQRLKAAGMPNHAIVDTGRNGVQGLREEWGNWCNVDGAGFGRPPSADTGLELADAFVWVKPGGESDGTSDSSAVRYDSFCGKPDAFQPSPEAGAWHQEYFEMLLRNSNPSLL |
| Enzyme Length | 398 |
| Uniprot Accession Number | B2AE04 |
| Absorption | |
| Active Site | ACT_SITE 125; /evidence=ECO:0000255|PROSITE-ProRule:PRU10056; ACT_SITE 170; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10057 |
| Activity Regulation | |
| Binding Site | BINDING 218; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 318; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 346; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 350; /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:23645193}; |
| 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. Hydrolyzes crystalline and amorphous cellulose but is inactive on hydroxyethyl cellulose, mannan, galactomannan, xyloglucan, arabinoxylan, arabinan, xylan, and pectin. {ECO:0000269|PubMed:23645193}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:23645193}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:23645193}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); 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 | PTM: Both N- and O-glycosylated. {ECO:0000269|PubMed:23645193}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,570 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.59 uM for cellotetraose {ECO:0000269|PubMed:23645193}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |