P37610
Gene name |
tauD (ssiD, yaiG, b0368, JW0360) |
Protein name |
Alpha-ketoglutarate-dependent taurine dioxygenase |
Names |
2-aminoethanesulfonate dioxygenase, Sulfate starvation-induced protein 3, SSI3 |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b0368 |
EC number |
1.14.11.17: With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
No variants for P37610
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P37610 | |||||
No associated diseases with P37610
1 regional properties for P37610
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TauD/TfdA-like domain | 7 - 272 | IPR003819 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.11.17 | With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| taurine dioxygenase complex | A protein complex capable of catalyzing the conversion of taurine and alpha-ketoglutarate to sulfite, aminoacetaldehyde and succinate under sulfur or cysteine starvation conditions. Its expression is repressed by the presence of sulfate or cysteine. In E. coli it is a homodimer or homotetramer of the protein TauD. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-oxoglutarate-dependent dioxygenase activity | Catalysis of the reaction: A + 2-oxoglutarate + O2 = B + succinate + CO2. This is an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from 2-oxoglutarate and one other donor, and one atom of oxygen is incorporated into each donor. |
| ferrous iron binding | Binding to a ferrous iron ion, Fe(II). |
| L-ascorbic acid binding | Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species. |
| taurine dioxygenase activity | Catalysis of the reaction: 2-oxoglutarate + O(2) + taurine = aminoacetaldehyde + CO(2) + succinate + sulfite. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| sulfur compound metabolic process | The chemical reactions and pathways involving the nonmetallic element sulfur or compounds that contain sulfur, such as the amino acids methionine and cysteine or the tripeptide glutathione. |
| taurine catabolic process | The chemical reactions and pathways resulting in the breakdown of taurine (2-aminoethanesulfonic acid), a sulphur-containing amino acid derivative important in the metabolism of fats. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSERLSITPL | GPYIGAQISG | ADLTRPLSDN | QFEQLYHAVL | RHQVVFLRDQ | AITPQQQRAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AQRFGELHIH | PVYPHAEGVD | EIIVLDTHND | NPPDNDNWHT | DVTFIETPPA | GAILAAKELP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| STGGDTLWTS | GIAAYEALSV | PFRQLLSGLR | AEHDFRKSFP | EYKYRKTEEE | HQRWREAVAK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NPPLLHPVVR | THPVSGKQAL | FVNEGFTTRI | VDVSEKESEA | LLSFLFAHIT | KPEFQVRWRW |
| 250 | 260 | 270 | 280 | ||
| QPNDIAIWDN | RVTQHYANAD | YLPQRRIMHR | ATILGDKPFY | RAG |