Q9HTY6
Gene name |
gshA |
Protein name |
Glutamate--cysteine ligase |
Names |
Gamma-ECS, GCS, Gamma-glutamylcysteine synthetase |
Species |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
KEGG Pathway |
pae:PA5203 |
EC number |
6.3.2.2: 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 Q9HTY6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9HTY6-F1 | Predicted | AlphaFoldDB |
No variants for Q9HTY6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9HTY6 | |||||
No associated diseases with Q9HTY6
1 regional properties for Q9HTY6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glutamate--cysteine ligase | 10 - 378 | IPR007370 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.2.2 | Acid--amino-acid ligases (peptide synthases) |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glutamate-cysteine ligase activity | Catalysis of the reaction: L-cysteine + L-glutamate + ATP = L-gamma-glutamyl-L-cysteine + ADP + 2 H(+) + phosphate. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| glutathione biosynthetic process | The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSDLLSRRLA | LLGAAANLPL | LTECLHGIER | ECLRVDSDGK | LALTPHPRAL | GSTLTHPQIT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TDYSEALLEF | ITPTETDVAD | TLGDLERIHR | FASSKLDGEY | LWSPSMPCEL | PDEESIPIAR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YGSSMIGRLK | YVYRKGLALR | YGKTMQCIAG | IHYNFSLPER | LWPLLRQAEG | SELSERDYQS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AAYIALIRNF | RRYSWLLMYL | FGASPALDAG | FLRGRPSQLE | RLDEHTLYLP | YATSLRMSDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GYQNNAQAGL | TPCYNDLQSY | IDSLRQAVST | PYPPYEKVGT | KQDGEWVQLN | TNILQIENEY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YSSIRPKRVT | YTGERPVQAL | AARGVQYVEV | RCLDINPFLP | LGIDLDEARF | LDAFLLFCAF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SDSPLLNGEC | SDATDNFLAV | VKEGRRPGLQ | LQRRGQPVEL | QVWANELLER | IADTAALLDR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ARGGEAHAAA | LAAQRAKVAD | AELTPSAQVL | KVMRERGESF | EAFSLRQSRE | HAEYFRQHPL |
| 490 | 500 | 510 | 520 | ||
| AAEEQARFEK | MASDSLAEQT | ELERDQDGDF | DTFVAAYQAS | ILGLISN |