Q9X1X4
Gene name |
TM_1639 |
Protein name |
Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit homolog |
Names |
Dihydroorotate oxidase B, electron transfer subunit homolog |
Species |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
KEGG Pathway |
tma:TM1639 |
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
3 structures for Q9X1X4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4YLF | X-ray | 230 A | A/C | 1-276 | PDB |
| 4YRY | X-ray | 240 A | A/C | 1-276 | PDB |
| AF-Q9X1X4-F1 | Predicted | AlphaFoldDB |
No variants for Q9X1X4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9X1X4 | |||||
No associated diseases with Q9X1X4
4 regional properties for Q9X1X4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Oxidoreductase FAD/NAD(P)-binding | 108 - 199 | IPR001433 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain | 9 - 96 | IPR008333 |
| domain | FAD-binding domain, ferredoxin reductase-type | 2 - 100 | IPR017927 |
| domain | Dihydroorotate dehydrogenase, electron transfer subunit, iron-sulphur cluster binding domain | 216 - 252 | IPR019480 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2 iron, 2 sulfur cluster binding | Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| 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. |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| pyrimidine nucleotide biosynthetic process | The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGGTALNEIV | KKVKIAEDVF | DFWIHSPSVS | KEARPGQFVV | IRLHEKGERI | PLTVADTKPE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EGLFRMVVKV | VGKTTHELSL | KKEGDTILDV | VGPLGNPSEI | ENYGNVLLVG | GGVGIATLYP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IAKALKEAGN | NITTVLGART | KDYLIMVDEF | KEISDVLLVT | DDGSAGMKGV | VTDAMDKLFR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ERKFDICWAV | GPTIMMKFCT | LKAREFGVPI | WVSLNPIMVD | GTGMCGACRV | TVSGQIKFAC |
| 250 | 260 | 270 | 280 | ||
| VDGPEFRGEE | VDWDELLKRL | AQYREQEKIS | YERFLKTAGE | SE |