Q9C9U3
PR
Gene name |
DOX2 (DIOX2, At1g73680, F25P22.10) |
Protein name |
Alpha-dioxygenase 2 |
Names |
Alpha DOX2, Fatty acid dioxygenase AlphaDOX2 |
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT1G73680 |
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 Q9C9U3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9C9U3-F1 | Predicted | AlphaFoldDB |
28 variants for Q9C9U3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| ENSVATH01532492 | 6 | S>F | No | 1000Genomes | |
| tmp_1_27707390_A_C | 10 | F>V | No | 1000Genomes | |
| ENSVATH05140329 | 19 | V>I | No | 1000Genomes | |
| ENSVATH01532487 | 52 | A>T | No | 1000Genomes | |
| ENSVATH14477098 | 71 | P>S | No | 1000Genomes | |
| ENSVATH05140319 | 78 | D>N | No | 1000Genomes | |
| ENSVATH01532485 | 113 | S>A | No | 1000Genomes | |
| ENSVATH13803878 | 116 | Q>L | No | 1000Genomes | |
| ENSVATH00141582 | 125 | S>T | No | 1000Genomes | |
| tmp_1_27706285_G_C | 133 | A>G | No | 1000Genomes | |
| tmp_1_27705772_C_T | 240 | G>R | No | 1000Genomes | |
| tmp_1_27705766_C_T | 242 | G>S | No | 1000Genomes | |
| ENSVATH14477079 | 286 | Y>C | No | 1000Genomes | |
| ENSVATH05140281 | 287 | P>Q | No | 1000Genomes | |
| ENSVATH13803862 | 389 | I>L | No | 1000Genomes | |
| ENSVATH01532463 | 394 | N>I | No | 1000Genomes | |
| ENSVATH05140279 | 394 | N>K | No | 1000Genomes | |
| ENSVATH01532463 | 394 | N>S | No | 1000Genomes | |
| ENSVATH05140278 | 401 | E>D | No | 1000Genomes | |
| tmp_1_27705050_T_G | 409 | I>L | No | 1000Genomes | |
| ENSVATH05140271 | 423 | A>G | No | 1000Genomes | |
| ENSVATH05140270 | 426 | L>I | No | 1000Genomes | |
| ENSVATH14477076 | 450 | N>I | No | 1000Genomes | |
| ENSVATH00141578 | 469 | I>M | No | 1000Genomes | |
| ENSVATH01532459 | 483 | G>R | No | 1000Genomes | |
| tmp_1_27704417_G_A | 567 | T>M | No | 1000Genomes | |
| ENSVATH05140263 | 592 | I>V | No | 1000Genomes | |
| ENSVATH00141565 | 598 | R>K | No | 1000Genomes |
No associated diseases with Q9C9U3
1 regional properties for Q9C9U3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AP2/ERF domain | 26 - 90 | IPR001471 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| dioxygenase activity | Catalysis of an oxidation-reduction (redox) reaction in which both atoms of oxygen from one molecule of O2 are incorporated into the (reduced) product(s) of the reaction. The two atoms of oxygen may be distributed between two different products. [DOI:10.1016/S0040-4020(03)00944-X, GOC:bf] |
| 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. |
| oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor. |
| peroxidase activity | Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid biosynthetic process | The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. |
| fatty acid metabolic process | The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
| leaf senescence | The last stage of leaf development during which programmed degradation of macromolecules and nutrient recycling take place. |
| long-chain fatty acid metabolic process | The chemical reactions and pathways involving long-chain fatty acids, A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. |
| oxylipin biosynthetic process | The chemical reactions and pathways resulting in the formation of any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids. |
| response to oxidative stress | 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O62664 | PTGS1 | Prostaglandin G/H synthase 1 | Bos taurus (Bovine) | PR |
| Q8HZR1 | PTGS1 | Prostaglandin G/H synthase 1 | Canis lupus familiaris (Dog) (Canis familiaris) | PR |
| Q9UPX0 | IGSF9B | Protein turtle homolog B | Homo sapiens (Human) | PR |
| P35354 | PTGS2 | Prostaglandin G/H synthase 2 | Homo sapiens (Human) | PR |
| P23219 | PTGS1 | Prostaglandin G/H synthase 1 | Homo sapiens (Human) | PR |
| P22437 | Ptgs1 | Prostaglandin G/H synthase 1 | Mus musculus (Mouse) | PR |
| Q05769 | Ptgs2 | Prostaglandin G/H synthase 2 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGFSPSSSWF | LHPQLHHVVS | KMSYFDAFLF | YIVHLVDKLG | LWHRFPVLLG | VAYLGLRRHL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HQRYNLVHVG | PINGQGYDTD | EFCYRTADGK | CNHPSDNTIG | SQGSFIGRNM | PPSTSQYGIL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DPHPSVVATK | LLARKRFIDN | GDQFNVIACS | WIQFMIHDWV | DHLEDTHQIE | LEAPEEVASG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CPLKSFKFLR | TKKVPTDDHH | KSGAVNTRTP | WWDGSVIYGN | DETGMRRVRV | FKDGKLKISG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DGLLERDERG | VPISGDIRNS | WSGFSLLQAL | FVKEHNSVCD | MLKERYPDFD | DEKLYRTARL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VTAAVIAKVH | TIDWTIELLK | TDTLTAGMRI | NWYGFFGKKV | KDMVGARFGP | LFSGLVGLKK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PNDHGVPYSL | TEEFVSVYRM | HCLLPETLIL | RDMNSENVDK | ENPAIEREIP | MTELIGKKAG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EKASKLGFEQ | LLVSMGHQSC | GALTLWNYPN | WMRNLVAQDI | DGEDRPHLID | MAALEIYRDR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ERGVPRYNEF | RKNLLMSPIS | KWEELTDDEE | AIKVLREVYE | DDIEKLDLNV | GLHAEKKIKG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FAISETAFFI | FLLVASRRLE | ADRFFTTNFN | EKTYTKEGLE | WVNTTETLKD | VIDRHFPRLT |
| 610 | 620 | 630 | |||
| DQWMRCSSAF | SVWGSDPNPK | NWVPLYLRSA | P |