| IED ID | IndEnz0008000592 |
| Enzyme Type ID | cellulase000592 |
| Protein Name |
Endo-1,4-beta-xylanase C Xylanase C EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase C 34 kDa xylanase Xylanase X34 |
| Gene Name | xlnC AN1818 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MVHLKTLAGSAVFASLATAAVLPRQSASLNDLFVAAGKSYFGTCSDQALLQNSQNEAIVASQFGVITPENSMKWDALEPSQGNFGWSGADYLVDYATQHNKKVRGHTLVWHSQLPSWVSSIGDANTLRSVMTNHINEVVGRYKGKIMHWDVVNEIFNEDGTFRNSVFYNLLGEDFVRIAFETARAADPDAKLYINDYNLDSASYAKTQAMASYVKKWLAEGVPIDGIGSQAHYSSSHWSSTEAAGALSSLANTGVSEVAITELDIAGAASSDYLNLLNACLNEQKCVGITVWGVSDKDSWRASDSPLLFDGNYQPKDAYNAIVNALS |
| Enzyme Length | 327 |
| Uniprot Accession Number | Q00177 |
| Absorption | |
| Active Site | ACT_SITE 154; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 262; /note=Nucleophile; /evidence=ECO:0000250 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. {ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:8917072}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 52 degrees Celsius. {ECO:0000269|PubMed:16844780}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.9. {ECO:0000269|PubMed:16844780}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Chain (1); Disulfide bond (1); Domain (1); Erroneous gene model prediction (2); Helix (16); Modified residue (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 | INDUCTION: Expressed in presence of xylan and repressed by glucose. {ECO:0000269|PubMed:8917072}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25043916}. |
| Modified Residue | MOD_RES 25; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000250 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1TA3; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,441 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |