| IED ID | IndEnz0008000485 |
| Enzyme Type ID | cellulase000485 |
| Protein Name |
Endo-1,4-beta-xylanase 2 Xylanase 2 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 2 Alkaline endo-beta-1,4-xylanase |
| Gene Name | xyn2 xln2 TRIREDRAFT_123818 |
| 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 | MVSFTSLLAGVAAISGVLAAPAAEVESVAVEKRQTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS |
| Enzyme Length | 223 |
| Uniprot Accession Number | G0RUP7 |
| Absorption | |
| Active Site | ACT_SITE 119; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01097; ACT_SITE 210; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01097 |
| Activity Regulation | |
| Binding Site | BINDING 106; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 110; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 121; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 155; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 159; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 169; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P36217; BINDING 204; /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:0000250|UniProtKB:P36217}; |
| 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. {ECO:0000250|UniProtKB:P36217}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:8975597}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:8975597}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01097}. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Domain (1); Glycosylation (2); Modified residue (1); Mutagenesis (2); Propeptide (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Reference proteome;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:0000269|PubMed:23291620}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8975597}. |
| Modified Residue | MOD_RES 34; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P36217 |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:8975597}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,069 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |