A6X191
Gene name |
gatB |
Protein name |
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
Names |
Asp/Glu-ADT subunit B |
Species |
Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi) |
KEGG Pathway |
oan:Oant_2279 |
EC number |
|
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 A6X191
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A6X191-F1 | Predicted | AlphaFoldDB |
No variants for A6X191
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A6X191 | |||||
No associated diseases with A6X191
No regional properties for A6X191
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A6X191 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP. |
| 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 |
| MSLIDTRIPE | PKRFISGATG | DWEVVIGMEV | HAQVTSESKL | FSGASTSFGA | EPNSNVSLVD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AAMPGMLPVI | NLECVKQAVR | TGIGLNAQIN | LKSVFDRKNY | FYPDLPQGYQ | ISQFKQPIVG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EGKIMISVGP | DNKGQFEDVE | IGIERLHLEQ | DAGKSMHDQH | PTMSYVDLNR | SGVALMEIVS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KPDLRSSDEA | RAYLTKLRTI | VRYLGTCDGN | MDEGSMRADV | NVSVRRPGGE | FGTRCEIKNV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NSIRFVGQAI | EYEARRQIAI | LEDGGSIDQE | TRLFDPVKGE | TRSMRSKEEA | HDYRYFPDPD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLPLEFDQAF | VDALAVDLPE | LPDVKKQRLV | EKQGISIYDA | SILVTEKAIA | DYYESVAAGR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DGKAAANWVI | NDLLGALNKA | GKDIEESPVS | PEQLGAVIDL | IKEGTISGKI | AKDLFEIVWN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EGGDPKKLVE | ERGMKQVTDT | GAIEKAVDDV | IAANPEKVEQ | AKAKPTLAGW | FVGQVMKATG |
| 490 | |||||
| GKANPQSVNE | LVKAKLGIEE |