| IED ID | IndEnz0010001824 |
| Enzyme Type ID | esterase001824 |
| Protein Name |
Bifunctional acetylxylan esterase/xylanase XynS20E Includes: Acetylxylan esterase EC 3.1.1.72 ; Endo-1,4-beta-xylanase Xylanase EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase |
| Gene Name | xynS20E |
| Organism | Neocallimastix patriciarum (Rumen fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Chytridiomycota Chytridiomycota incertae sedis Neocallimastigomycetes Neocallimastigales Neocallimastigaceae Neocallimastix Neocallimastix patriciarum (Rumen fungus) |
| Enzyme Sequence | MRLGVALSTIAVLLTATSARNLDKRQWGWPNFGGGNGGNGGNGGKTINDYKREQGAGRDIHVYAPSNLAPNSPLLLSLHGMDQDPNYQQSNTHWETLADSEGFVVVYPRGGTGMSTWDIQGTKDTQWVSQIIDQMKKEYNIDTKRVYLSGFSMGGMFTYHAMSQIANKIAAFAPCSGPNVFGASKAQRPVPIFHVHGTNDDVLNYQQVEGFLKNYRDQFHCPSQADTKTNYPNRENPNATLYTWGPCDKGVYIKHLKLQGRGHSPSSADIQDIWDFVSQWTVDGPVSASGNGGGNTTPTNPSTGGNGNGNGGGNTTPTNPSTGGNGNGNGGSTDKCSSNITKQGYKCCASNCEVVYTDSDGDWGVENDQWCGCGNRVTVGSGTCSAKILQQGYKCCPSGCIIYYTDEDGTWGVNGEEWCGCGSGSSSTGGGNDAPSSGSGYQGANGTNFCNNAKHSGESVTVTSNKVGDINGIGYELWADSGNNSATFYDDGSFSCSFQRAKDYLCRSGLSFDSTKTHKQIGHIYAEFKLVKQNIQNVDYSYVGIYGWTRNPLVEFYVVDNWLSQWRPGDWVGNKKHGDFTIGGAQYTVYENTRYGPSIDGDTNFKQYFSIRQQPRDCGTIDITAHFEQWEKLGMTMGKMHEAKVLGEAGSNNGGTSGTADFPFAKVYVKN |
| Enzyme Length | 671 |
| Uniprot Accession Number | B8YG19 |
| Absorption | |
| Active Site | ACT_SITE 152; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 555; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 648; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:19690850}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19690850}; |
| DNA Binding | |
| EC Number | 3.1.1.72; 3.2.1.8 |
| Enzyme Function | FUNCTION: Bifunctional acetylxylan esterase/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. Degrades xylan from acetylxylan, beechwood, birchwood, and oat spelt, and releases acetate from 4-methylumbelliferyl acetate and beta-D-xylose tetraacetate. No activity is observed against carboxy methyl cellulose, beta-glucan, p-nitrophenol acetate, p-nitrophenol laurate, p-nitrophenol myristate, p-nitrophenol, palmitate, or beta-naphthol acetate. {ECO:0000269|PubMed:19690850}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 58 degrees Celsius for acetylxylan esterase activity, and 49 degrees Celsius for endo-1,4-beta-xylanase activity.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.8 for acetylxylan esterase activity, and 5.8 for endo-1,4-beta-xylanase activity.; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (3); Glycosylation (4); Region (2); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19690850}. |
| 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 | 72,469 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.48 mg/ml for birchwood xylan for endo-1,4-beta-xylanase activity; KM=16.72 mg/ml for birchwood xylan for acetylxylan esterase activity; Vmax=5.15 umol/min/mg enzyme toward birchwood xylan for acetylxylan esterase activity; Vmax=153.27 umol/min/mg enzyme toward birchwood xylan for Endo-1,4-beta-xylanase activity; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.72; |