A3QAK2
Gene name |
glnE |
Protein name |
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme |
Names |
ATP:glutamine synthetase adenylyltransferase, ATase |
Species |
Shewanella loihica (strain ATCC BAA-1088 / PV-4) |
KEGG Pathway |
slo:Shew_0628 |
EC number |
2.7.7.42: Nucleotidyltransferases |
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 A3QAK2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A3QAK2-F1 | Predicted | AlphaFoldDB |
No variants for A3QAK2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A3QAK2 | |||||
No associated diseases with A3QAK2
4 regional properties for A3QAK2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glutamate-ammonia ligase adenylyltransferase, repeated domain | 41 - 276 | IPR005190-1 |
| domain | Glutamate-ammonia ligase adenylyltransferase, repeated domain | 558 - 814 | IPR005190-2 |
| domain | PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase | 307 - 444 | IPR013546-1 |
| domain | PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase | 834 - 927 | IPR013546-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.42 | Nucleotidyltransferases |
| 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| [glutamate-ammonia-ligase] adenylyltransferase activity | Catalysis of the reaction: ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]. |
| [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase | Catalysis of the reaction: adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O = AMP + [L-glutamate:ammonia ligase (ADP-forming)]. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| metabolic process | The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation. |
| regulation of glutamine family amino acid metabolic process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving amino acids of the glutamine family, comprising arginine, glutamate, glutamine and proline. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MENMSEQALP | HEVNQVAEQH | WQRLAEAWPD | ISEQLTPEQT | KELKTIFGLS | DFVAEQLCRH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PNWIVSLFEG | QLSMLARDSF | SSELHSILAG | ANDEEQVKAI | LRRYRNRQMV | RLAWRDFLGY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AELNDSLLDL | SALAEALIIA | ARDWLYGQMC | QQYGTPCDSE | GNPQPLMILG | MGKLGGRELN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FSSDIDLIFT | FPEHGETQGG | RRSQDNQQFF | IRMGQRLVNL | LNQVTVDGFV | YRVDMRLRPY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GESGPLVVSF | SGLEDYYQEQ | GRDWERYAMV | KARALGPWSA | YSDELHDMLR | PFVYRRYIDF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SAIESLRKMK | QLITQEVRRR | RLTDNIKLGA | GGIREVEFVV | QSFQLIRGGR | EPALRQQSLF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GAIDTLYKLG | QLEYLAVDEL | KQSYLMLRRV | ENLLQAIGDQ | QTQTLPQHLL | DWQRLCFALG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MAGEAELRTH | IESAMAKIHR | YFKETVGGQE | SDEVAEQWTA | QLWSLVDDED | AEALLKEHGV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EESELWPALK | SWRGTVAKRT | IGPRGRETLD | KLMPWLLQEF | IQLPTPTKAF | LPVSKVLDQI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LTRTTYLELL | FENPGARQQL | VSLCMASPWI | GEQLAKFPML | LDELIDPAQL | YDTTSLDDYP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SELRQYLLRV | PEEDMEQQME | ALRQFKLSQQ | LKIAAADVTG | VLPVMQVSDH | LTFLAEAIIE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QVVLQAWQQV | SKRHGTPSYL | APEEMGFAVI | GYGKAGGLEL | GYGSDLDLVF | LHNYTRDKYP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DAQQTNGDRP | IDIGHFYLKL | AQRILHLFST | RTTSGELYEV | DMRLRPSGAS | GLLVSEIEYF |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GSYQREEAWT | WEHQALVRAR | FLFGDNRLAA | RFSELRADVL | AMERDKAELA | KEVREMRQKM |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RTHLLKVDEG | CFDLKQSPGG | IADIEFIAQY | LVLANTHDHP | ELAIWSDNVR | IFEVLSELEL |
| 910 | 920 | 930 | 940 | 950 | |
| LPHLSAQHLT | QAYCYLRDES | HRLTLQQAPG | QLPQESVDLH | VQRVLAIYEQ | VLNNGQ |