| IED ID | IndEnz0008000487 |
| Enzyme Type ID | cellulase000487 |
| Protein Name |
1,4-beta-D-glucan cellobiohydrolase xynA EC 3.2.1.91 Beta-glucancellobiohydrolase xynA Exocellobiohydrolase xynA Exoglucanase xynA |
| Gene Name | xynA |
| Organism | Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Enzyme Sequence | MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSNLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSTNNSNTGIGNHGSCCAELDIWEANSISEALTPHPCDTPGLTVCTADDCGGTYSSNRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPFTVVTQFVTDDGTSSGSLSEIRRYYVQNGVVIPQPSSKISGISGNVINSDFCAAELSAFGETASFTNHGGLKNMGSALEAGMVLVMSLWDDYSVNMLWLDSTYPANETGTPGAARGSCPTTSGNPKTVESQSGSSYVVFSDIKVGPFNSTFSGGTSTGGSTTTTASGTTSTKASTTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL |
| Enzyme Length | 529 |
| Uniprot Accession Number | Q8WZJ4 |
| Absorption | |
| Active Site | ACT_SITE 234; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 239; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Cellobiose inhibits xynA at high concentrations. {ECO:0000269|PubMed:22776993}. |
| Binding Site | |
| 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:22776993}; |
| DNA Binding | |
| EC Number | 3.2.1.91 |
| Enzyme Function | FUNCTION: 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:22776993}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:22776993}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.0-4.5. {ECO:0000269|PubMed:22776993}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Region (4); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12664153}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,048 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.238 mM for 4-nitrophenyl-beta-D-cellobioside {ECO:0000269|PubMed:22776993}; KM=0.57 mM for 4-nitrophenyl-beta-D-lactopyranoside {ECO:0000269|PubMed:22776993}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |