Q2HWK7
Gene name |
DES |
Protein name |
Acyl-lipid omega-13 desaturase |
Names |
CrDES, Omega13 fatty acid desaturase |
Species |
Chlamydomonas reinhardtii (Chlamydomonas smithii) |
KEGG Pathway |
cre:CHLRE_10g453600v5 |
EC number |
1.14.19.12: With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
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 Q2HWK7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2HWK7-F1 | Predicted | AlphaFoldDB |
No variants for Q2HWK7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2HWK7 | |||||
No associated diseases with Q2HWK7
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.19.12 | With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-lipid omega-(9-4) desaturase | Catalysis of the reaction: linoleoyl- + 2 ferrocytochrome b5 + O2 + 2 H(+) <=> pinolenoyl- |
| alpha-linolenate delta5 desaturase activity | Catalysis of the reaction: alpha-linolenate + O2 + a reduced electron acceptor = coniferonate + 2 H2O + an oxidized electron acceptor. |
| 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 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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| linoleic acid metabolic process | The chemical reactions and pathways involving linoleic acid, an unsaturated omega-6 fatty acid that has the molecular formula C18H32O2. |
| 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. |
| unsaturated fatty acid metabolic process | The chemical reactions and pathways involving 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 |
| MCRPTDSDSG | PALPSIPHQY | WIIHGATYDL | ASYIKSHPGG | DEAILLGRGR | DCTELFEQYH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VLNNKHLRVL | ERFRVTLPAA | KVATNNLKED | MVSTISAFEG | EEADAAAVVG | IQQPAAPARV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AHQSDPFYED | IKAMVRAHGN | TKMSAPFVIL | HCLHVVGLIW | SMKLWWQGAF | ISAFILPYFL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| WVLCAAMVHD | GGHFAHSKRP | LVNKLLTHTG | ALFTNSVGCW | YLQHNILHHS | YTNLVGKDGD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LDSHHPYMRI | HPEQSMLPAN | IHHAVRFFSH | LIMYNFAHIG | LTMISPLSYF | RGVAAQKKGT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ADAKQAQDAQ | TVAQYHSTVM | LQLVTVGAFY | ITPFLRFDFS | RALLLTLLPT | FMMSVAFMVI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AQVSHIQMDA | EAPSADLEKL | HWARRMALTS | VDYSQESTLW | AYLTIGLNMQ | SLHHIVPGVS |
| 430 | 440 | 450 | 460 | 470 | |
| YSQLPRLYPA | YRAICEKHGI | KLLERRNLAH | AFWTHLQTLW | VLSKTHSFVE | VARKLA |