P0A9U8
Gene name |
ydiO (b1695, JW5275) |
Protein name |
Probable acyl-CoA dehydrogenase YdiO |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b1695 |
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 P0A9U8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0A9U8-F1 | Predicted | AlphaFoldDB |
No variants for P0A9U8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0A9U8 | |||||
No associated diseases with P0A9U8
5 regional properties for P0A9U8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Acyl-CoA dehydrogenase, conserved site | 123 - 135 | IPR006089-1 |
| conserved_site | Acyl-CoA dehydrogenase, conserved site | 335 - 354 | IPR006089-2 |
| domain | Acyl-CoA oxidase/dehydrogenase, middle domain | 121 - 216 | IPR006091 |
| domain | Acyl-CoA dehydrogenase/oxidase C-terminal | 228 - 376 | IPR009075 |
| domain | Acyl-CoA dehydrogenase/oxidase, N-terminal | 6 - 107 | IPR013786 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-CoA dehydrogenase activity | Catalysis of the reaction: acyl-CoA + oxidized |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 1-butanol biosynthetic process | The chemical reactions and pathways resulting in the formation of 1-butanol, an alkyl primary alcohol with the formula C4H10O. |
| fatty acid beta-oxidation using acyl-CoA dehydrogenase | A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDFSLTEEQE | LLLASIRELI | TTNFPEEYFR | TCDQNGTYPR | EFMRALADNG | ISMLGVPEEF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GGIPADYVTQ | MLALMEVSKC | GAPAFLITNG | QCIHSMRRFG | SAEQLRKTAE | STLETGDPAY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALALTEPGAG | SDNNSATTTY | TRKNGKVYIN | GQKTFITGAK | EYPYMLVLAR | DPQPKDPKKA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FTLWWVDSSK | PGIKINPLHK | IGWHMLSTCE | VYLDNVEVEE | SDMVGEEGMG | FLNVMYNFEM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ERLINAARST | GFAECAFEDA | ARYANQRIAF | GKPIGHNQMI | QEKLALMAIK | IDNMRNMVLK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VAWQADQHQS | LRTSAALAKL | YCARTAMEVI | DDAIQIMGGL | GYTDEARVSR | FWRDVRCERI |
| 370 | 380 | ||||
| GGGTDEIMIY | VAGRQILKDY | QNK |