| IED ID | IndEnz0004000108 |
| Enzyme Type ID | xylanase000108 |
| Protein Name |
Endo-1,4-beta-xylanase 3 Xylanase 3 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 3 |
| Gene Name | xyn3 TRIREDRAFT_120229 |
| Organism | Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
| Enzyme Sequence | MKANVILCLLAPLVAALPTETIHLDPELAALRANLTERTADLWDRQASQSIDQLIKRKGKLYFGTATDRGLLQREKNAAIIQADLGQVTPENSMKWQSLENNQGQLNWGDADYLVNFAQQNGKSIRGHTLIWHSQLPAWVNNINNADTLRQVIRTHVSTVVGRYKGKIRAWDVVNEIFNEDGTLRSSVFSRLLGEEFVSIAFRAARDADPSARLYINDYNLDRANYGKVNGLKTYVSKWISQGVPIDGIGSQSHLSGGGGSGTLGALQQLATVPVTELAITELDIQGAPTTDYTQVVQACLSVSKCVGITVWGISDKDSWRASTNPLLFDANFNPKPAYNSIVGILQ |
| Enzyme Length | 347 |
| Uniprot Accession Number | G0RA32 |
| Absorption | |
| Active Site | ACT_SITE 176; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01096; ACT_SITE 282; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01096 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000250|UniProtKB:Q9P973}; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose. Produces xylobiose and xylotriose as the main degradation products. {ECO:0000250|UniProtKB:Q9P973}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01096}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (10); Chain (1); Disulfide bond (1); Domain (1); Helix (16); Modified residue (1); Propeptide (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9P973}. |
| Modified Residue | MOD_RES 46; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:Q9P973 |
| Post Translational Modification | PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q9P973}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4XV0; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 38,076 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |