Q5U4U6
Gene name |
tdo2 |
Protein name |
Tryptophan 2,3-dioxygenase |
Names |
TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:495495 |
EC number |
1.13.11.11: With incorporation of two atoms of oxygen |
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
1 structures for Q5U4U6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5U4U6-F1 | Predicted | AlphaFoldDB |
No variants for Q5U4U6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5U4U6 | |||||
No associated diseases with Q5U4U6
No regional properties for Q5U4U6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5U4U6 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.13.11.11 | With incorporation of two atoms of oxygen |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| metal ion binding | Binding to a metal ion. |
| tryptophan 2,3-dioxygenase activity | Catalysis of the reaction: L-tryptophan + O2 = N-formyl-L-kynurenine. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein homotetramerization | The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits. |
| tryptophan catabolic process to kynurenine | The chemical reactions and pathways resulting in the breakdown of tryptophan into other compounds, including kynurenine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSGCPFMAKK | HHFTFSELSL | EDKHEDNSQE | GLNKASKGGL | IYGDYLQLDK | VLNAQELQSE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKGNKIHDEH | LFIVTHQAYE | LWFKQILWEL | DSVREIFQNG | HVRDERNMLK | VVARIHRISM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ILKLLVEQFS | VLETMTAMDF | FDFRDYLSPA | SGFQSLQFRL | LENKIGVPEI | LRVPYNRRHY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RDNFKGETNE | LLLRSEQEPT | LLGLVEAWLE | RTPGLEEEGF | HFWGKLEVNI | FRALEEELQA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AKTKPDSEDK | EEHLAELQKQ | KELFGALFDE | RRHEHLLSKG | ERRLSYKALK | GALMINFYRE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EPRFQVPFQL | LTSLMEIDTL | MTKWRYNHVC | MVHRMIGSKA | GTGGSSGYQY | LRSTVSDRYK |
| 370 | 380 | 390 | 400 | ||
| VFVDLFNLST | YLVPRHWVPR | LNPSIHKFLY | TAECCDSSYF | SSDDSD |