P17714
Gene name |
ASNS |
Protein name |
Asparagine synthetase [glutamine-hydrolyzing] |
Names |
Glutamine-dependent asparagine synthetase |
Species |
Mesocricetus auratus (Golden hamster) |
KEGG Pathway |
|
EC number |
6.3.5.4: Carbon--nitrogen ligases with glutamine as amido-N-donor |
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 P17714
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P17714-F1 | Predicted | AlphaFoldDB |
No variants for P17714
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P17714 | |||||
No associated diseases with P17714
4 regional properties for P17714
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aspartyl/asparaginy/proline hydroxylase | 591 - 745 | IPR007803 |
| domain | Aspartyl beta-hydroxylase/Triadin domain | 43 - 108 | IPR007943 |
| repeat | Tetratricopeptide repeat | 341 - 374 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 454 - 487 | IPR019734-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.4 | Carbon--nitrogen ligases with glutamine as amido-N-donor |
| 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 |
|---|---|
| asparagine synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glutamine metabolic process | The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid. |
| L-asparagine biosynthetic process | The chemical reactions and pathways resulting in the formation of asparagine, (2S)-2-amino-3-carbamoylpropanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MCGIWALFGS | DDCLSVQCLS | AMKIAHRGPD | AFRFENVNGY | TNCCFGFHRL | AVVDPLFGMQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PIRVKKYPYL | WLCYNGEIYN | HKALQQRFEF | EYQTNVDGEI | ILHLYDKGGI | EQTICMLDGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FAFILLDTAN | KKVFLGRDTY | GVRPLFKAMT | EDGFLAVCSE | AKGLVSLKHS | TTPFLKVEPF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LPGHYEVLDL | KPNGKVASVE | MVKYHHCRDE | PLHALYDSVE | KLFPGFELET | VKSNLRILFD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NAVRKRLMTD | RRIVCLLSGG | LDSSLVASSL | LKQLKEAQVQ | YPLQTFAIGM | EDSPDLLAAR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KVANYIGSEH | HEVLFNSEEG | IQALDEVIFS | LETYDITTVR | ASVGMYLISK | YIRKNTDSVV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IFSGEGSDEL | TQGYIYFHKA | PSPEKAEEES | ERLLKELYLF | DVLRADRTTA | AHGLELRVPF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LDHRFSSYYL | SLPPEMRVPK | NGIEKHLLRE | TFEDSNLLPK | EILWRPKEAF | SDGITSVKNS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WFKILQDYVE | HQVDDAMMAT | AAQKFPFNTP | KTKEGYFYRQ | IFEHHYPGRA | DWLTHYWMPK |
| 550 | 560 | ||||
| WINATDPSAR | TLTHYKSAAK | A |