Q5EBG2
Gene name |
tdo2 |
Protein name |
Tryptophan 2,3-dioxygenase |
Names |
TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase |
Species |
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
KEGG Pathway |
xtr:548450 |
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 Q5EBG2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5EBG2-F1 | Predicted | AlphaFoldDB |
No variants for Q5EBG2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5EBG2 | |||||
No associated diseases with Q5EBG2
No regional properties for Q5EBG2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5EBG2 | |||
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. |
3 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 acetyl-CoA | The chemical reactions and pathways resulting in the breakdown of tryptophan into other compounds, including acetyl-CoA. |
| tryptophan catabolic process to kynurenine | The chemical reactions and pathways resulting in the breakdown of tryptophan into other compounds, including kynurenine. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P48775 | TDO2 | Tryptophan 2,3-dioxygenase | Homo sapiens (Human) | PR |
| P48776 | Tdo2 | Tryptophan 2,3-dioxygenase | Mus musculus (Mouse) | PR |
| P21643 | Tdo2 | Tryptophan 2,3-dioxygenase | Rattus norvegicus (Rat) | PR |
| A7MBU6 | tdo2a | Tryptophan 2,3-dioxygenase A | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| Q7SY53 | tdo2b | Tryptophan 2,3-dioxygenase B | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSGCPFMGKK | HHFNFSELSL | EDKNEDSSQE | GLNKASKGGL | IYGDYLQLDK | VLNAQELQSE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKGNKIHDEH | LFIVTHQAYE | LWFKQILWEL | DSVREIFQNG | HVRDERNMLK | VVTRIHRISM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ILKLLVEQFS | VLETMTAMDF | FDFRDYLSPA | SGFQSLQFRL | LENKIGVPEI | LRVPYNRRHY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RDNFKGETNE | LLLKSEQELT | LLGLVEAWLE | RTPGLEEEGF | HFWGKLEANI | FRGLEEELQT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VKTKPDSEEK | EEQLAELQKQ | KELFGALFDE | RRHEHLLSKG | ERRLSYKALK | GALMIYFYRE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EPRFQVPFQL | LTSLMDIDTL | MTKWRYNHVC | MVHRMIGSKA | GTGGSSGYQY | LRSTVSDRYK |
| 370 | 380 | 390 | 400 | ||
| VFVDLFNLST | YLVPRHWVPR | LNPSIHKFLY | TAECCDSSYF | SSDDSD |