IED ID | IndEnz0008000457 |
Enzyme Type ID | cellulase000457 |
Protein Name |
Endo-1,4-beta-xylanase A Xylanase A EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase A Endo-1,4-beta-xylanase GH10 A FoXyn10a Xylanase III |
Gene Name | FOXG_17421 |
Organism | Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium oxysporum species complex Fusarium oxysporum (Fusarium vascular wilt) Fusarium oxysporum f. sp. lycopersici Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) |
Enzyme Sequence | AASGLEAAMKAAGKQYFGTALTVRNDQGEIDIINNKNEIGSITPENAMKWEAIQPNRGQFNWGPADQHAAAATSRGYELRCHTLVWHSQLPSWVANGNWNNQTLQAVMRDHINAVMGRYRGKCTHWDVVNEALNEDGTYRDSVFLRVIGEAYIPIAFRMALAADPTTKLYYNDYNLEYGNAKTEGAKRIARLVKSYGLRIDGIGLQAHMTSESTPTQNTPTPSRAKLASVLQGLADLGVDVAYTELDIRMNTPATQQKLQTNADAYARIVGSCMDVKRCVGITVWGISDKYSWVPGTFPGEGSALLWNDNFQKKPSYTSTLNTINRR |
Enzyme Length | 327 |
Uniprot Accession Number | B3A0S5 |
Absorption | |
Active Site | ACT_SITE 131; /note="Proton donor"; /evidence="ECO:0000269|PubMed:22751658"; ACT_SITE 245; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10061, ECO:0000269|PubMed:22751658" |
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; Evidence={ECO:0000269|PubMed:9291571}; |
DNA Binding | |
EC Number | 3.2.1.8 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of the internal glycosidic bonds in heteroxylans, releasing mainly xylobiose and xylotriose. Most active on oat-spelt xylan. {ECO:0000269|PubMed:9291571}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:9291571}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|PubMed:9291571}; |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Beta strand (11); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (14); Turn (4) |
Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:9291571}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 3U7B; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 36,198 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=1.22 mmol/min/mg enzyme {ECO:0000269|PubMed:9291571}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |