O57740
Gene name |
pyrC |
Protein name |
Dihydroorotase |
Names |
DHOase |
Species |
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
KEGG Pathway |
pho:PH1963 |
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 O57740
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O57740-F1 | Predicted | AlphaFoldDB |
No variants for O57740
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O57740 | |||||
No associated diseases with O57740
4 regional properties for O57740
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Dihydroorotase, conserved site | 58 - 66 | IPR002195-1 |
| conserved_site | Dihydroorotase, conserved site | 273 - 284 | IPR002195-2 |
| domain | Amidohydrolase-related | 51 - 222 | IPR006680-1 |
| domain | Amidohydrolase-related | 271 - 386 | 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 |
| MTQVDLVVVG | KFLFKEKIID | GSIGIEDDKI | AKFSLRELKG | DKKIKVEKGK | IILPGLIDVH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VHLRDFNESY | KETIASGTKA | AIHGGITTVF | DMPNTKPPIM | DEKTLKLREL | IFKKKSYSDY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALGFLIAGNE | PAKADFYKIF | MGASTGGIYS | KNFEEDYKKA | PDIVSVHAEE | YELINRYPER |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PPIVEVVAIK | KALQASKKMK | KPLHICHVST | KDGLKEILKA | NIPWVSFEVT | PHHLFLTRRD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YERSKLLKVY | PPLRDEEDRR | YLWENLKSIP | IIASDHAPHT | LEDKEAGAAG | LPGLETEVAL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLDAVNKGMI | TIWDIVAKMS | INPARIFKIK | NKGWEEGKDA | DLIVVDMKKE | WTIKAENFYT |
| 370 | 380 | 390 | 400 | 410 | |
| KANWTPYEGW | KVKGKVIMTI | LRGEVVMEDD | EIIGKPRGER | IVKEGNAQGN | LGSSQEH |