Q9Y1W0
Gene name |
fadA (des5-1, DDB_G0285211) |
Protein name |
Delta(5) fatty acid desaturase A |
Names |
Delta-5 fatty acid desaturase A |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0285211 |
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 Q9Y1W0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9Y1W0-F1 | Predicted | AlphaFoldDB |
No variants for Q9Y1W0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9Y1W0 | |||||
No associated diseases with Q9Y1W0
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-CoA delta5-desaturase activity | Catalysis of the reaction: acyl-CoA + reduced acceptor + O2 = delta5-acyl-CoA + acceptor + 2 H2O. |
| metal ion binding | Binding to a metal ion. |
| 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. |
| oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced to two molecules of water. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid metabolic process | The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
| lipid metabolic process | The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. |
| response to heat | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| unsaturated fatty acid biosynthetic process | The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MYYSNKMSKV | ITGKQYSWSE | LAKHNTENDC | WVAVDGKVYD | ITRWVPLHPG | GKEVLLLAAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RDVTNLFESY | HPMSDKPTSI | LKNYEIGYIS | SYEHPKFVQK | SDFYKTLKER | VRKHFKATDQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DPQMAVSIFS | RLALVYLLVF | VTYYLAHYTS | NNFYLNCFLA | IVYALCNSLF | SMHMMHDSCH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AAISHYPGVW | KWMGASFDFV | TGASFLSWCH | QHVIGHHIYT | NVRNADPDLG | QGEVDFRIVT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PFQTRSWYHK | YQHIYAPLLY | GIYTLKYRTQ | DWEAFVKDGK | NGAIRVSVAT | NFDKAAYVIG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KLSFVFFRFI | LPLRYHSFTD | LICYFLIAEF | VFGWYLTINF | QVSHVAEDLK | FFATPERPDE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PSQINEDWAI | LQLKTTQDYG | HGSLLCTFFS | GSLNHQVVHH | LFPSIAQDFY | PQLVPIVKEV |
| 430 | 440 | 450 | 460 | ||
| CKEHNITYHI | KPNFTEAIMS | HINYLYKMGN | DPDYVKKPLA | SKDD |