| IED ID | IndEnz0004000022 |
| Enzyme Type ID | xylanase000022 |
| Protein Name |
Endo-1,4-beta-xylanase D Xylanase D EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase D |
| Gene Name | xynD |
| Organism | Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Enzyme Sequence | MTLVKSILLALAAGHVAQAQLNTAAKAAGLLYFGTAVDNPDLSDSKYLVNLETADFGQITPANAMKWQPTEPSQGSYTFTQGDQIASLAKSNNDYLRCHNLVWYNQLPSYITSGSWTNATLIAALKEHINGVVTHYKGQCYAWDVVNEALNEDGTYRQNVFYQHIGEAYIPIAFAAAAAADPNAKLYYNDYNIEYAGAKATGAQGIVKLIQAAGGRIDGVGLQSHFIVGQTPSLATQKANMAAFTALGVDVAITELDIRMTLPDTSALQTQQSTDYQTTTTACVQTKGCVGITLWDYTDKYSWVPGTFSGQGDACPWDSNYNKKPAYYGILAGLQSGSGSSSSTSSTTLITTTTPTASSSTTSATTTSATSGAAHWGQCGGIGWSGPTICVSPYTCQVLNPYYSQCL |
| Enzyme Length | 407 |
| Uniprot Accession Number | Q5ZNB1 |
| Absorption | |
| Active Site | ACT_SITE 148; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 255; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by wheat xylanase inhibiting protein I (XIP-I). {ECO:0000269|Ref.1}. |
| 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:0000269|PubMed:21466666, ECO:0000269|Ref.1}; |
| 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. Shows an endo-mode of action on xylan forming mainly xylobiose and short-chain xylooligosaccharides (XOS). {ECO:0000269|PubMed:21466666}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.2-5.2 for birchwood xylan and 4.0 for CM cellulose. {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (1); Region (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,235 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mg/ml for birchwood xylan {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1}; KM=11 mg/ml for insoluble fractions of wheat arabinoxylans {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1}; Vmax=130 umol/min/mg enzyme toward birchwood xylan {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1}; Vmax=535 umol/min/mg enzyme toward insoluble fractions of wheat arabinoxylans {ECO:0000269|PubMed:21466666, ECO:0000269|Ref.1}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |