A6QAK6
Gene name |
purL |
Protein name |
Phosphoribosylformylglycinamidine synthase subunit PurL |
Names |
FGAM synthase, Formylglycinamide ribonucleotide amidotransferase subunit II, FGAR amidotransferase II, FGAR-AT II, Glutamine amidotransferase PurL, Phosphoribosylformylglycinamidine synthase subunit II |
Species |
Sulfurovum sp (strain NBC37-1) |
KEGG Pathway |
sun:SUN_1565 |
EC number |
6.3.5.3: 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 A6QAK6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A6QAK6-F1 | Predicted | AlphaFoldDB |
No variants for A6QAK6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A6QAK6 | |||||
No associated diseases with A6QAK6
5 regional properties for A6QAK6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PurM-like, C-terminal domain | 208 - 359 | IPR010918-1 |
| domain | PurM-like, C-terminal domain | 577 - 711 | IPR010918-2 |
| domain | PurM-like, N-terminal domain | 87 - 194 | IPR016188-1 |
| domain | PurM-like, N-terminal domain | 458 - 562 | IPR016188-2 |
| domain | Phosphoribosylformylglycinamidine synthase, linker domain | 14 - 53 | IPR041609 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.3 | 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 |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| phosphoribosylformylglycinamidine synthase activity | Catalysis of the reaction: N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + ATP + H(2)O = 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate + ADP + 2 H(+) + phosphate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' IMP biosynthetic process | The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSQPVENLDE | VLKNHKLSKE | EYEDILRILD | GRHPNIVEIG | IFSAMWSEHC | SYKSSKKYLN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GFPTKAPWVI | QGPGENAGVI | DIGDGMAAVF | KMESHNHPSF | IEPFQGAATG | VGGILRDIFT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MGARPVANLN | ALRFGRVRGD | SDINKYQRHL | VRGVVDGIGS | YGNCMGVPTI | GGEVSFDESY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NGNILVNAFS | LGLVKSDEIF | LGVASGIGNP | VMYVGSKTGR | DGLGGAVMSS | DSFTEESKSL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RPTVQVGDPF | TEKLLLEACL | ELFKTDAIIG | IQDMGAAGLT | SSAFEMAGKT | GAGLIMHLDK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VPAREEGMTP | YDFMLSESQE | RMLICAKKGR | EQEIIDIFEK | WELDVAVIGE | VTDTERMELF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WYGDKVCDMP | IAPVSEEAPI | LDRPVARPAY | LNEVIAKTVD | DYAKVDDQEA | YEKLLAPLEV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VDKAWVYNQY | DSMVQTNTTK | HPGSLDASCI | RIKENGRALA | MSSDCNPRYC | YIDPKGGAAL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AVVESGRNVA | MSGARPLSIT | DCLNYGNPEN | PEVMWQFAQG | CEGIKEACLE | LNTPVVSGNV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SLYNETNGVS | VFPTPAIAMV | GLNDDQNKVL | PSVFQHEGNN | IVLIGETKGE | FGGSLYIKEL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FGETVGTLPS | FDYKTELKLW | ELVIEANKIG | LLESAKDVNV | GGIAIALSKM | AAVSSKGITV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KASVSNSRDI | FDESQSRALL | EVADADLEEL | LDMAAGLGLK | AEVIGKIGGE | EVKVNDVALP |
| 730 | |||||
| LEKVKDVYFN | TFKRTIEQDL |