IED ID | IndEnz0008000046 |
Enzyme Type ID | cellulase000046 |
Protein Name |
1,4-beta-D-glucan cellobiohydrolase CEL6A EC 3.2.1.91 Beta-glucancellobiohydrolase CEL6A Exocellobiohydrolase CEL6A Exoglucanase CEL6A |
Gene Name | CEL6A Pa_0_1250 PODANS_0_1250 |
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 | MAKRLLLTAALAATTLAAPVIEERQNCGSVWSQCGGQGWTGATCCASGSTCVAQNQWYSQCLPGSQVTTTAQAPSSTRTTTSSSSRPTSSSISTSAVNVPTTTTSAGASVTVPPGGGASSTASYSGNPFLGVQQWANSYYSSEVHTLAIPSLTGPMATKAAAVAKVPSFQWMDRNVTVDTLFSGTLADIRAANRAGANPPYAGIFVVYDLPDRDCAAAASNGEWAIADGGAAKYKAYIDRIRHHLVQYSDIRTILVIEPDSLANMVTNMNVPKCQGAANTYKELTVYALKQLNLPNVAMYLDAGHAGWLGWPANIGPAAELFAGIYKDAGRPTSLRGLATNVANYNGWSLSSAPSYTTPNPNFDEKRFVQAFSPLLTAAGFPAHFITDTGRSGKQPTGQLEWGHWCNAIGTGFGPRPTTDTGLDIEDAFVWIKPGGECDGTSDTTAARYDHHCGFADALKPAPEAGQWFQAYFEQLLTNANPPF |
Enzyme Length | 484 |
Uniprot Accession Number | B2ABX7 |
Absorption | |
Active Site | ACT_SITE 260; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q9C1S9, ECO:0000255|PROSITE-ProRule:PRU10057"; ACT_SITE 439; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q9C1S9, ECO:0000255|PROSITE-ProRule:PRU10056" |
Activity Regulation | |
Binding Site | BINDING 171; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 173; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 305; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 308; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 344; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 405; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 433; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9C1S9; BINDING 437; /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 55 degrees Celsius. {ECO:0000269|PubMed:23645193}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:23645193}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Binding site (8); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Region (3); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Cellulose degradation;Disulfide bond;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..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 51,054 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.7 uM for cellotetraose {ECO:0000269|PubMed:23645193}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |