A1UEC6
Gene name |
Mkms_1985 |
Protein name |
Uncharacterized oxidoreductase Mkms_1985 |
Names |
|
Species |
Mycobacterium sp (strain KMS) |
KEGG Pathway |
mkm:Mkms_1985 |
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 A1UEC6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1UEC6-F1 | Predicted | AlphaFoldDB |
No variants for A1UEC6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1UEC6 | |||||
No associated diseases with A1UEC6
3 regional properties for A1UEC6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aldo/keto reductase, conserved site | 124 - 141 | IPR018170-1 |
| conserved_site | Aldo/keto reductase, conserved site | 228 - 243 | IPR018170-2 |
| domain | NADP-dependent oxidoreductase domain | 21 - 260 | IPR023210 |
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 |
| MGAPLVALND | GNSIPQVGLG | VWQTPPEDTE | RAVAAALAAG | YRHVDTAAAY | GNEEQTGRAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AQSGLDRSQV | YLVTKLWNSE | QGYDATLAAF | EASVDRLGVD | YLDLYLIHWP | VPEKNLFVDT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FKAFARLRED | GRIRSIGVSN | FEPEHLRVLI | DSTGIVPAVN | QIELHPLLPQ | RELRELHAQL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GIATEAWSPL | GQGSLLAHPT | VTGVAESHGK | TAAQALIRWH | MQLGNIVIPK | SVNPQRIESN |
| 250 | 260 | 270 | |||
| FDVFDFELSE | QDMASISSLE | DGSRLGPDPK | TFNFTG |