Q2SCJ3
Gene name |
guaA |
Protein name |
GMP synthase [glutamine-hydrolyzing] |
Names |
GMP synthetase, Glutamine amidotransferase |
Species |
Hahella chejuensis (strain KCTC 2396) |
KEGG Pathway |
hch:HCH_04942 |
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 Q2SCJ3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2SCJ3-F1 | Predicted | AlphaFoldDB |
No variants for Q2SCJ3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2SCJ3 | |||||
No associated diseases with Q2SCJ3
5 regional properties for Q2SCJ3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GMP synthase, C-terminal | 214 - 526 | IPR001674 |
| domain | GMP synthase, glutamine amidotransferase | 10 - 206 | IPR004739 |
| domain | Glutamine amidotransferase | 12 - 201 | IPR017926 |
| domain | NAD/GMP synthase | 215 - 293 | IPR022310 |
| domain | GMP synthetase ATP pyrophosphatase domain | 209 - 401 | 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 |
| MSENIHSHRI | LILDFGSQYT | QLIARRVREI | GVYCEIYPFD | MSEADIREFN | PKGVILAGGP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ESVTELGSPR | APECLFNMDL | PLLGICYGMQ | TMAEQMGGKV | AGSNVREFGY | AQVKIERSED |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GLFENIKDHV | AEDGKPLLDV | WMSHGDKVVA | LPEGFVISAS | TPSAPIAAMQ | HESKPWFGVQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FHPEVTHTLQ | GRRMLERFLV | NICGCKQLWT | PGRIIEDAIT | QVRNQVGQDK | VLLGLSGGVD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SSVVAALLHR | AIGDQLTCVF | VDNGLLRLHE | GDQVMDMFAK | NMGIKVVRAN | AQDQFLSKLA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GENDPERKRK | IIGHTFIEVF | DAEAAKIKDV | KWLAQGTIYP | DVIESAAAKT | GKAHVIKSHH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NVGGLPEDME | MQLVEPLREL | FKDEVRKIGL | ELGLPYDMVY | RHPFPGPGLG | VRILGEVKKE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YADILREADA | IFIEELHRAE | LYHKVSQAFA | VFLPVKSVGV | VGDARRYEYV | IALRAVETID |
| 490 | 500 | 510 | 520 | ||
| FMTARWAHLP | YELLEKISNR | IINEISGVSR | VVYDVSSKPP | ATIEWE |