Q2PG45
Gene name |
TBXAS1 (CYP5, CYP5A1, QccE-11311) |
Protein name |
Thromboxane-A synthase |
Names |
TXA synthase, TXS, Cytochrome P450 5A1, Hydroperoxy icosatetraenoate dehydratase |
Species |
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
KEGG Pathway |
|
EC number |
4.2.1.152: Hydro-lyases |
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 Q2PG45
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2PG45-F1 | Predicted | AlphaFoldDB |
No variants for Q2PG45
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2PG45 | |||||
No associated diseases with Q2PG45
1 regional properties for Q2PG45
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Cytochrome P450, conserved site | 472 - 481 | IPR017972 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.152 | Hydro-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| 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. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| 12-hydroxyheptadecatrienoic acid synthase activity | Catalysis of the reaction: prostaglandin H2 = 12-hydroxyheptadecatrienoic acid (HHT) + malonaldehyde (MDA). |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| hydroperoxy icosatetraenoate dehydratase activity | A hydroperoxy icosatetraenoate <=> an oxoicosatetraenoate + H(2)O. |
| iron ion binding | Binding to an iron (Fe) ion. |
| monooxygenase activity | Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water. |
| oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor. |
| thromboxane-A synthase activity | Catalysis of the reaction: prostaglandin H(2) = thromboxane A(2). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| icosanoid metabolic process | The chemical reactions and pathways involving icosanoids, any of a group of C20 polyunsaturated fatty acids. |
| prostaglandin biosynthetic process | The chemical reactions and pathways resulting in the formation of prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEALGFLKLE | VNGPMVTVAL | SVALLALLKW | YSTSAFSRLE | KLGLRHPKPS | PFIGNLMFFR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QGFWESQMEL | RKLYGPLCGY | YLGRRMFIVI | SEPDMIKQVL | VENFSNFTNR | MASGLEFKSV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ADSVLFLRDK | RWEEVRGALM | SAFSPEKLNE | MTPLISQACD | LLLAHLKRYA | ESGDAFDIQR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CYRNYTTDVV | ASVAFGTPVD | SQQAPEDPFV | KHCKRFFEFC | IPRPILVLLL | SFPSIMVPLA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RILPNKNRDE | LNGFFNKLIR | NVIALRDQQA | AEERRRDFLQ | MVLDARHSAS | PVGVQDFDMV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GDVFSSTRCK | PNPSRQHQAG | PMARPLTVDE | IVGQAFIFLI | AGYEIVTNTL | SFATYLLATN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PDCQEKLLRE | VDLFKEKHMV | PEFCSLEEGL | PYLDMVIAET | LRMYPPAFRF | TREAAQDCEV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LGQRIPAGAV | LEMAVGALHH | DPEHWPSPET | FNPERFTAEA | QQQHRPFTYL | PFGAGPRSCL |
| 490 | 500 | 510 | 520 | 530 | |
| GVRLGLLEVK | LTLLHVLHKF | QFQACPETQV | PLQLESKSAL | GPKNGVYIKI | VSR |