| IED ID | IndEnz0004000262 |
| Enzyme Type ID | xylanase000262 |
| Protein Name |
Xylan alpha- 1- 2 -glucuronosidase EC 3.2.1.131 Alpha-glucuronidase |
| Gene Name | aguA |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MTAGYEPCWLRYERKDQYSRLRFEEIVAKRTSPIFQAVVEELQKGLRSMMEIEPQVVQEVNETANSIWLGTLEDEEFERPLEGTLVHPEGYVIRSDVDDGPFRIYIIGKTDAGVLYGVFHFLRLLQMGENIAQLSIIEQPKNRLRMINHWDNMDGSIERGYAGRSIFFVDDQFVKQNQRIKDYARLLASVGINAISINNVNVHKTETKLITDHFLPDVAEVADIFRTYGIKTFLSINYASPIEIGGLPTADPLDPEVRRWWKETAKRIYQYIPDFGGFVVKADSEFRPGPFTYGRDHAEGANMLAEALAPFGGLVIWRCFVYNCQQDWRDRTTDRAKAAYDHFKPLDGQFRENVILQIKNGPMDFQVREPVSPLFGAMPKTNQMMEVQITQEYTGQQKHLCFLIPQWKEVLDFDTYAKGKGSEVKKVIDGSLFDYRYSGIAGVSNIGSDPNWTGHTLAQANLYGFGRLAWNPDLSAEEIANEWVVQTFGDDSQVVETISWMLLSSWRIYENYTSPLGVGWMVNPGHHYGPNVDGYEYSHWGTYHYADRDGIGVDRTVATGTGYTAQYFPENAAMYESLDTCPDELLLFFHHVPYTHRLHSGETVIQHIYNTHFEGVEQAKQLRKRWEQLKGKIDEKRYHDVLERLTIQVEHAKEWRDVINTYFYRKSGIDDQYGRKIYR |
| Enzyme Length | 679 |
| Uniprot Accession Number | Q09LY5 |
| Absorption | |
| Active Site | ACT_SITE 285; /note=Proton donor; /evidence=ECO:0000269|PubMed:14573597; ACT_SITE 364; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:14573597; ACT_SITE 392; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:14573597 |
| Activity Regulation | ACTIVITY REGULATION: The metal cations Ni(2+), K(+) and Zn(2+) show some inhibition of the activity, and Ag(+), Hg(2+) and Cu(2+) shows very significant inhibition even at relatively low ion concentrations. {ECO:0000269|PubMed:11358519}. |
| Binding Site | BINDING 201; /note=beta-D-glucuronic acid; /evidence=ECO:0000250; BINDING 281; /note=Substrate; BINDING 318; /note=Substrate; BINDING 335; /note=Substrate; BINDING 359; /note=Substrate; BINDING 386; /note=Substrate; /evidence=ECO:0000250; BINDING 510; /note=Substrate; /evidence=ECO:0000250; BINDING 540; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.; EC=3.2.1.131; |
| DNA Binding | |
| EC Number | 3.2.1.131 |
| Enzyme Function | FUNCTION: Alpha-glucuronidase 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. It catalyzes the cleavage of alpha-1,2-glycosidic bond of the 4-O-methyl-D-glucuronic acid side chain of xylan and releases 4-O-methylglucuronic acid from xylan. {ECO:0000269|PubMed:11358519}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. The enzyme is stable up to 70 degrees Celsius and lost 70% of its activity at 75 degrees Celsius. {ECO:0000269|PubMed:11358519}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6. It retains about 40% of its activity at pH 4.5 and 7.5. {ECO:0000269|PubMed:11358519}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (23); Binding site (8); Chain (1); Helix (27); Mutagenesis (6); Region (1); Site (2); Turn (9) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1K9E; 1K9F; 1MQP; 1MQR; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,484 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for aldotetraouronic acid (at 55 degrees Celsius) {ECO:0000269|PubMed:11358519}; Vmax=42 umol/min/ug enzyme with aldotetraouronic acid as substrate (at 55 degrees Celsius) {ECO:0000269|PubMed:11358519}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.139; |