| IED ID | IndEnz0004000001 |
| Enzyme Type ID | xylanase000001 |
| Protein Name |
Endo-1,4-beta-xylanase 2 EX 2 Xylanase 2 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 2 Alkaline endo-beta-1,4-xylanase |
| Gene Name | xyn2 M419DRAFT_124931 |
| 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 | MVSFTSLLAGVAAISGVLAAPAAEVESVAVEKRQTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS |
| Enzyme Length | 223 |
| Uniprot Accession Number | P36217 |
| Absorption | |
| Active Site | ACT_SITE 119; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374"; ACT_SITE 210; /note="Proton donor"; /evidence="ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374" |
| Activity Regulation | |
| Binding Site | BINDING 106; /note=Substrate; /evidence=ECO:0000269|PubMed:24419374; BINDING 110; /note=Substrate; /evidence=ECO:0000269|PubMed:24419374; BINDING 121; /note=Substrate; /evidence=ECO:0000269|PubMed:24419374; BINDING 155; /note=Substrate; /evidence=ECO:0000269|PubMed:24419374; BINDING 159; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:24419374; BINDING 169; /note=Substrate; /evidence=ECO:0000269|PubMed:24419374; BINDING 204; /note=Substrate; /evidence=ECO:0000269|PubMed:24419374 |
| 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.5}; |
| 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.5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747). {ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:19556747, ECO:0000269|PubMed:7988708, ECO:0000269|Ref.5}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.5 (PubMed:1369024). Stable from pH 3.0 to 8.5 at room temperature and from pH 4.0 to 7.5 at 40 degrees Celsius (Ref.5). {ECO:0000269|PubMed:1369024, ECO:0000269|Ref.5}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01097}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (13); Binding site (7); Chain (1); Domain (1); Frameshift (1); Glycosylation (2); Helix (1); Modified residue (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Induced by D-xylose, dependent on the cellulase and xylanase regulator xyr1. Repressed by glucose through negative regulation by the crabon catabolite repressor cre1. {ECO:0000250|UniProtKB:G0RUP7}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.5}. |
| Modified Residue | MOD_RES 34; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:16790934" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | Neutron diffraction (1); Electron microscopy (1); X-ray crystallography (41) |
| Cross Reference PDB | 1ENX; 1RED; 1REE; 1REF; 1XYO; 1XYP; 2D97; 2D98; 2DFB; 2DFC; 3LGR; 4HK8; 4HK9; 4HKL; 4HKO; 4HKW; 4S2D; 4S2F; 4S2G; 4S2H; 4XPV; 4XQ4; 4XQD; 4XQW; 5K7P; 5ZF3; 5ZH0; 5ZH9; 5ZII; 5ZIW; 5ZKZ; 5ZO0; 6JUG; 6JWB; 6JXL; 6JZP; 6K9O; 6K9R; 6K9W; 6K9X; 6KVV; 6KW9; 6KWC; 6KWD; 6KWE; 6KWF; 6KWG; 6KWH; |
| Mapped Pubmed ID | 16510975; 20606256; 21301107; 23519813; 28192420; 33128114; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,069 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mg/ml for beechwood (unsubstituted) xylan {ECO:0000269|PubMed:1369024}; KM=13.8 mg/ml for birchwood xylan {ECO:0000269|PubMed:17416973}; KM=3.0 mg/ml for acetylated glucuronoxylan {ECO:0000269|Ref.5}; KM=3.8 mg/ml for deacetylated glucuronoxylan {ECO:0000269|Ref.5}; KM=6.8 mg/ml for unsubstituted xylan {ECO:0000269|Ref.5}; KM=73 uM for xylohexaose {ECO:0000269|PubMed:17475200}; KM=136 uM for xylopentaose {ECO:0000269|PubMed:17475200}; Vmax=1600 umol/min/mg enzyme for beechwood xylan {ECO:0000269|PubMed:1369024}; Vmax=336 umol/min/mg enzyme for birchwood xylan {ECO:0000269|PubMed:17416973}; Note=kcat is 68 sec(-1) with xylohexaose, 50.3 sec(-1) with xylopentaose, 0.162 sec(-1) with xylotetraose and 0.045 sec(-1) with xylotriose as substrate. {ECO:0000269|PubMed:17475200}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |