Q6LU31
Gene name |
guaA |
Protein name |
GMP synthase [glutamine-hydrolyzing] |
Names |
GMP synthetase, Glutamine amidotransferase |
Species |
Photobacterium profundum (strain SS9) |
KEGG Pathway |
ppr:PBPRA0781 |
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 Q6LU31
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6LU31-F1 | Predicted | AlphaFoldDB |
No variants for Q6LU31
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6LU31 | |||||
No associated diseases with Q6LU31
5 regional properties for Q6LU31
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GMP synthase, C-terminal | 238 - 550 | IPR001674 |
| domain | GMP synthase, glutamine amidotransferase | 40 - 229 | IPR004739 |
| domain | Glutamine amidotransferase | 42 - 225 | IPR017926 |
| domain | NAD/GMP synthase | 248 - 320 | IPR022310 |
| domain | GMP synthetase ATP pyrophosphatase domain | 233 - 425 | 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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
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 (glutamine-hydrolyzing) activity | Catalysis of the reaction: ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate + 2H(+). |
| pyrophosphatase activity | Catalysis of the hydrolysis of a pyrophosphate bond (diphosphate bond) between two phosphate groups. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| glutamine metabolic process | The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTSTNIHDQ | RILILDFGSQ | YTQLIARRIR | EIGVYCELWS | WDVDEADIRD | FNPNGIILSG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPESVTGDES | PRAPQYVFEA | GVPVFGVCYG | MQTMAEQLGG | KVAGSSMREF | GYAQVEIVEP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TSFFKNIEDA | VAEDGNGLLD | VWMSHGDKVV | EIPSDFVKVA | QTDTCPFAAI | ANEEKHFYGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QFHPEVTHTR | QGMRIIENFV | LNICGCENLW | TSANIIEDAI | ANIKEQVGDD | EVILGLSGGV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DSSVVAMLLH | RAIGDKLTCV | FVDNGLLRLN | EGEQVMDMFG | DHFGLNIVHV | KAEDRFLNAL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AGENDPEAKR | KIIGHAFIDV | FDEESKKLKN | AKWLAQGTIY | PDVIESAASK | NGKAHVIKSH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HNVGGLPDDM | EMGLVEPLRE | LFKDEVRKIG | LELGLPYNML | YRHPFPGPGL | GVRVLGEVKK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EYCDLLRRAD | AIFIEELHSA | DLYNKVSQAF | TVFLPVRSVG | VMGDGRKYDW | VVSLRAVETI |
| 490 | 500 | 510 | 520 | ||
| DFMTAHWAHL | PYDFLGKVSN | RIINEVDGIS | RVVYDISGKP | PATIEWE |