Q5L431
Gene name |
gltX |
Protein name |
Glutamate--tRNA ligase |
Names |
Glutamyl-tRNA synthetase, GluRS |
Species |
Geobacillus kaustophilus (strain HTA426) |
KEGG Pathway |
gka:GK0083 |
EC number |
6.1.1.17: Ligases forming aminoacyl-tRNA and related compounds |
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 Q5L431
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5L431-F1 | Predicted | AlphaFoldDB |
No variants for Q5L431
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5L431 | |||||
No associated diseases with Q5L431
3 regional properties for Q5L431
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| binding_site | Serine hydroxymethyltransferase, pyridoxal phosphate binding site | 281 - 297 | IPR019798 |
| domain | Serine hydroxymethyltransferase-like domain | 42 - 136 | IPR039429-1 |
| domain | Serine hydroxymethyltransferase-like domain | 171 - 442 | IPR039429-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.17 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glutamate-tRNA ligase activity | Catalysis of the reaction: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). |
| tRNA binding | Binding to a transfer RNA. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| glutamyl-tRNA aminoacylation | The process of coupling glutamate to glutamyl-tRNA, catalyzed by glutamyl-tRNA synthetase. The glutamyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamic acid-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKEVRVRYA | PSPTGHLHIG | GARTALFNYL | FARHHGGKMI | VRIEDTDIER | NVEGGEKSQL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ENLKWLGIDY | DESIDQDGGY | GPYRQTERLD | IYRKYVNELL | EQGHAYKCFC | TPEELERERE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AQRAAGIAAP | QYSGKCRHLT | PEQVAELEAQ | GKPYTIRLKV | PEGKTYEFYD | LVRGKVVFES |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KDVGGDWVIV | KANGIPTYNF | AVVIDDHLME | ISHVFRGEEH | LSNTPKQLMV | YEYFGWEPPQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FAHLTLIVNE | QRKKLSKRDE | SIIQFVSQYK | ELGYLPEAMF | NFFALLGWSP | EGEEEIFTKD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELIRMFDVSR | LSKSPSMFDT | KKLTWMNNQY | IKKLDLDRLV | ELALPHLVKA | GRLPADMTDE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QRQWARDLIA | LYQEQMSYGA | EIVPLSELFF | KEEIDYEDEA | RQVLAEEQVP | AVLSTFLESV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RELEPFTADE | IKAAIKAVQK | ATGQKGKKLF | MPIRAAVTGQ | THGPELPFAI | QLLGKEKVIE |
| RLERALQEKF |