Detail Information for IndEnz0008000046
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