P35668
Gene name |
gss |
Protein name |
Glutathione synthetase |
Names |
GSH synthetase, GSH-S, Glutathione synthase |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:394329 |
EC number |
6.3.2.3: Acid--amino-acid ligases (peptide synthases) |
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 P35668
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P35668-F1 | Predicted | AlphaFoldDB |
No variants for P35668
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P35668 | |||||
No associated diseases with P35668
1 regional properties for P35668
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glutathione synthase, substrate-binding domain | 205 - 302 | IPR004887 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.2.3 | Acid--amino-acid ligases (peptide synthases) |
| 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 |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glutathione binding | Binding to glutathione; a tripeptide composed of the three amino acids cysteine, glutamic acid and glycine. |
| glutathione synthase activity | Catalysis of the reaction: L-gamma-glutamyl-L-cysteine + ATP + glycine = ADP + glutathione + 2 H(+) + phosphate. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADLWDDIYN | DTKLLEELAP | IAIDAALLQG | VLMRTKESPN | SSDVVSFAPF | ALLPSPVPKA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LFEQAKCVQE | DFNTLVDRIS | QDTSFLEQVL | SSTIKVDDFI | RRLFAIHKQV | QQEDCTQEVF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LGINRSDYMF | DCRDDGTPAL | KQIEINTIAA | SFGGLASRTP | AVHQHVLKFL | RKSEESSSIL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TNDAVEGIGW | GIAHAWALYG | SVDATVMFLV | ENEQRNILDQ | RFIEAELCKR | NVRVIRRRLA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVFERGTLDE | ERHLFIDGYE | VAVAYFRTGY | VPQDYTEQDW | EARLMLERSR | AVKCPDVPTQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LVGTKKVQQE | LSRPQILEKF | LPDKPEAVAR | IRETFTGLYS | LDIGEEGDEA | VRVALANPDQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FVLKPQREGG | GNNLYGEELK | EKLQECKDSE | ERTSYILMDK | INPKPLKNCL | LRAGGRVQIS |
| 430 | 440 | 450 | 460 | 470 | |
| ECISELGMFG | VYVRHRDQMI | YYDQVGHLLR | TKAIEHSDGG | VAAGVAVLDN | PYLV |