Q9JXR2
Gene name |
guaA (NMB1920) |
Protein name |
GMP synthase [glutamine-hydrolyzing] |
Names |
GMP synthetase, Glutamine amidotransferase |
Species |
Neisseria meningitidis serogroup B (strain MC58) |
KEGG Pathway |
nme:NMB1920 |
EC number |
6.3.5.2: 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 Q9JXR2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9JXR2-F1 | Predicted | AlphaFoldDB |
No variants for Q9JXR2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9JXR2 | |||||
No associated diseases with Q9JXR2
5 regional properties for Q9JXR2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GMP synthase, C-terminal | 203 - 521 | IPR001674 |
| domain | GMP synthase, glutamine amidotransferase | 6 - 194 | IPR004739 |
| domain | Glutamine amidotransferase | 8 - 190 | IPR017926 |
| domain | NAD/GMP synthase | 204 - 286 | IPR022310 |
| domain | GMP synthetase ATP pyrophosphatase domain | 198 - 390 | IPR025777 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.2 | 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 |
|---|---|
| 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. |
| GMP synthase activity | Catalysis of the reaction: ATP + XMP + NH4(+) = AMP + diphosphate + GMP + 2H(+). |
| pyrophosphatase activity | Catalysis of the hydrolysis of a pyrophosphate bond (diphosphate bond) between two phosphate groups. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glutamine metabolic process | The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid. |
| GMP biosynthetic process | The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTQDKILILD | FGSQVTQLIA | RRVREAHVYC | ELHSFDMPLD | EIKAFNPKGI | ILSGGPNSVY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ESDYQADTGI | FDLGIPVLGI | CYGMQFMAHH | LGGEVQPGNQ | REFGYAQVKT | IDSELTRGIQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DGEPNTLDVW | MSHGDKVSKL | PDGFAVIGNT | PSCPIAMMEN | AEKQFYGIQF | HPEVTHTKQG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RALLNRFVLD | ICGAQPGWTM | PNYIEEAVAK | IREQVGSDEV | ILGLSGGVDS | SVAAALIHRA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IGDQLTCVFV | DHGLLRLNES | KMVMDMFARN | LGVKVIHVDA | EGQFMAKLAG | VTDPEKKRKI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IGAEFIEVFD | AEEKKLTNAK | WLAQGTIYPD | VIESAGAKTK | KAHAIKSHHN | VGGLPENMKL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLLEPLRDLF | KDEVRELGVA | LGLPREMVYR | HPFPGPGLGV | RILGEVKKEY | ADLLRQADDI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FIQELRNTTD | ENGTSWYDLT | SQAFAVFLPV | KSVGVMGDGR | TYDYVIALRA | VITSDFMTAH |
| 490 | 500 | 510 | 520 | ||
| WAELPYSLLG | KVSNRIINEV | KGINRVVYDV | SGKPPATIEW | E |