Q8U4A0
Gene name |
pyrC |
Protein name |
Dihydroorotase |
Names |
DHOase |
Species |
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
KEGG Pathway |
pfu:PF0189 |
EC number |
3.5.2.3: In cyclic amides |
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 Q8U4A0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8U4A0-F1 | Predicted | AlphaFoldDB |
No variants for Q8U4A0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8U4A0 | |||||
No associated diseases with Q8U4A0
4 regional properties for Q8U4A0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Dihydroorotase, conserved site | 55 - 63 | IPR002195-1 |
| conserved_site | Dihydroorotase, conserved site | 270 - 281 | IPR002195-2 |
| domain | Amidohydrolase-related | 48 - 144 | IPR006680-1 |
| domain | Amidohydrolase-related | 199 - 383 | IPR006680-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.5.2.3 | In cyclic amides |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| dihydroorotase activity | Catalysis of the reaction: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate + H(+). |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' UMP biosynthetic process | The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEVVLEGKFL | LDKRTIEGYI | GIEDGKISKI | SLREIKGDHK | IKVDKGKVIL | PGLIDVHVHL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RDFEESYKES | IESGTKAAVH | GGITVVFDMP | NTKPPIMDEK | TLKLREHLFK | RKSYADYALG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FLLAGNKPVE | ADFYKIFMGA | STGGIYSKNF | EEDYIRALDI | VSIHAEDYEI | IQKYPERPPI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AEIRAIERVI | EAVKTHKKPA | HICHISTAKG | LKLLLDSRLE | MLSFEVTPHH | LFLTRSDYDK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NPLLKVYPPL | RSEEDRIALW | KNIDKVPVIA | SDHAPHTLED | KEAGAAGLPG | LETEVPLLLD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AVNKGLITLQ | DIVEKMHINP | IKIFGIENKG | FEKGKDADFT | IVDMKREWTI | RADNLYTKAG |
| 370 | 380 | 390 | 400 | 410 | |
| WTPYEGWRVK | GKVIMTIIRG | EVVMEEDEII | GKPRGERIVK | KGKHRRNLGS | SEEH |