P0AG85
Gene name |
yghA (Z4356, ECs3887) |
Protein name |
Uncharacterized oxidoreductase YghA |
Names |
|
Species |
Escherichia coli O157:H7 |
KEGG Pathway |
ecs:ECs_3887 |
EC number |
|
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 P0AG85
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0AG85-F1 | Predicted | AlphaFoldDB |
No variants for P0AG85
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0AG85 | |||||
No associated diseases with P0AG85
1 regional properties for P0AG85
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Short-chain dehydrogenase/reductase, conserved site | 186 - 214 | IPR020904 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSHLKDPTTQ | YYTGEYPKQK | QPTPGIQAKM | TPVPDCGEKT | YVGSGRLKDR | KALVTGGDSG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IGRAAAIAYA | REGADVAISY | LPVEEEDAQD | VKKIIEECGR | KAVLLPGDLS | DEKFARSLVH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EAHKALGGLD | IMALVAGKQV | AIPDIADLTS | EQFQKTFAIN | VFALFWLTQE | AIPLLPKGAS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IITTSSIQAY | QPSPHLLDYA | ATKAAILNYS | RGLAKQVAEK | GIRVNIVAPG | PIWTALQISG |
| 250 | 260 | 270 | 280 | 290 | |
| GQTQDKIPQF | GQQTPMKRAG | QPAELAPVYV | YLASQESSYV | TAEVHGVCGG | EHLG |