A0Q2Q0
Gene name |
gatA |
Protein name |
Glutamyl-tRNA(Gln) amidotransferase subunit A |
Names |
Glu-ADT subunit A |
Species |
Clostridium novyi (strain NT) |
KEGG Pathway |
cno:NT01CX_0431 |
EC number |
6.3.5.7: 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 A0Q2Q0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A0Q2Q0-F1 | Predicted | AlphaFoldDB |
No variants for A0Q2Q0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A0Q2Q0 | |||||
No associated diseases with A0Q2Q0
1 regional properties for A0Q2Q0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Amidase signature domain | 24 - 463 | IPR023631 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.7 | 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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| glutamyl-tRNA(Gln) amidotransferase complex | A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| translation | The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MELFNKTAHE | LIDMIKSKEV | KVEEVVKSYI | ARTECIDEKI | GAYLYLSKES | ALKEAKLLDE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KIQRGEKLKG | LWGVPVGIKD | NISVSGMQNT | CASKILENYI | SPYDATVISR | LKENNGIILG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLNMDEFAMG | SSNENSAFKI | VRNPWDLERI | PGGSSGGSTA | AVASREIPLS | LGSETGGSVR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QPAALCGVVG | LKPTYGRISR | YGVISFASTL | DQVGTIGRDV | TDCAILTEVI | SGFDKRDSTS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ARVAVPNYKE | SLKKDLTGIR | IGLPKEFFKE | DLDESIRKQI | EDAIKILEKN | GAEIKICSLP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LAEYSLSAYY | IISTAEASSN | LARIDGIRYG | RRINTLDKHE | DIYIQSRNEG | FGEEVKKRIM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LGTYVLSKGC | YEKYYEKALK | VRTLIKEDFK | RVLKEVDAII | TPTSKVTAFK | FGERTKEVLS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MYSSDEYTVP | ASIAGLPAIS | IPCGFSKGLP | VGFQLIGDYF | REDILFNIGY | SYEQSTDFHK |
| IMAKL |