| IED ID | IndEnz0004000014 |
| Enzyme Type ID | xylanase000014 |
| Protein Name |
Endo-1,4-beta-xylanase 1 EX 1 Xylanase 1 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 1 Acidic endo-beta-1,4-xylanase |
| Gene Name | xyn1 M419DRAFT_38418 |
| Organism | Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (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 ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) |
| Enzyme Sequence | MVAFSSLICALTSIASTLAMPTGLEPESSVNVTERGMYDFVLGAHNDHRRRASINYDQNYQTGGQVSYSPSNTGFSVNWNTQDDFVVGVGWTTGSSAPINFGGSFSVNSGTGLLSVYGWSTNPLVEYYIMEDNHNYPAQGTVKGTVTSDGATYTIWENTRVNEPSIQGTATFNQYISVRNSPRTSGTVTVQNHFNAWASLGLHLGQMNYQVVAVEGWGGSGSASQSVSN |
| Enzyme Length | 229 |
| Uniprot Accession Number | P36218 |
| Absorption | |
| Active Site | ACT_SITE 126; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 215; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
| Activity Regulation | |
| Binding Site | BINDING 117; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 128; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 160; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 164; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 174; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 209; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:1369024, ECO:0000269|Ref.3}; |
| 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 (PubMed:1369024, Ref.3). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). {ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:7988708, ECO:0000269|Ref.3}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5-4.0 (PubMed:1369024). Stable from pH 2.5 to 8.5 at room temperature and from pH 2.5 to 4.5 at 40 degrees Celsius (Ref.3). {ECO:0000269|PubMed:1369024, ECO:0000269|Ref.3}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01097}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Binding site (6); Chain (1); Domain (1); Glycosylation (1); Helix (1); Propeptide (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Induced by D-xylose and L-arabinose, dependent on the cellulase and xylanase regulator xyr1. Repressed by glucose through negative regulation by the crabon catabolite repressor cre1. {ECO:0000250|UniProtKB:G0R947}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1XYN; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,583 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mg/ml for beechwood (unsubstituted) xylan {ECO:0000269|PubMed:1369024}; KM=14.8 mg/ml for acetylated glucuronoxylan {ECO:0000269|Ref.3}; KM=22.3 mg/ml for deacetylated glucuronoxylan {ECO:0000269|Ref.3}; KM=18.9 mg/ml for unsubstituted xylan {ECO:0000269|Ref.3}; Vmax=100 umol/min/mg enzyme for beechwood xylan {ECO:0000269|PubMed:1369024}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |