O67691
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 |
Aquifex aeolicus (strain VF5) |
KEGG Pathway |
aae:aq_1836 |
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 O67691
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O67691-F1 | Predicted | AlphaFoldDB |
No variants for O67691
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O67691 | |||||
No associated diseases with O67691
5 regional properties for O67691
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PurM-like, C-terminal domain | 193 - 347 | IPR010918-1 |
| domain | PurM-like, C-terminal domain | 576 - 716 | IPR010918-2 |
| domain | PurM-like, N-terminal domain | 80 - 181 | IPR016188-1 |
| domain | PurM-like, N-terminal domain | 432 - 558 | IPR016188-2 |
| domain | Phosphoribosylformylglycinamidine synthase, linker domain | 8 - 45 | 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 |
| MERVWEAYGL | TEEEYRKILK | TLKREPNHVE | LGVLGALWSE | HCSYKSSKKH | LKKFPTKAEW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VVQGPGENAG | VVKIDEKVWV | AFKVESHNHP | SYIEPFHGAA | TGVGGIIRDV | LSMGARPIAL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ADSLRFGEFN | YHETKRLVKG | VVSGISFYGN | CIGVPTVAGE | TVFEPSYKTN | PLVNAFCLGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IPAGRMYRAR | ATREGQLLFL | IGSSTGRDGI | FGAVMASGEF | SEDVEEKRPN | VQIGDPYFGK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KLVEAIMEIV | EKDLIVGMQD | LGAAGLAGSA | SEIAAKSEKG | VELYLENVPL | REKDMNPYEI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLSESQERML | LVVEEENVEK | VKEIANKWHL | EGAVVGKITD | DDTFRAYYKG | ELVAELPVSL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IVDEAPVYDR | PYKEPEYMKE | VRNFNQEELP | QTDVKEALKK | LLSSPNISCK | EWVYTQYDYQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VGTNTLLIPG | HDAAVLRLKW | VLRPELTTEK | GIAISSEGNG | RMVYLNPYEG | GKFVVAEVCR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NLACVGAKPL | AITDCLNFGN | PERPEIMWQF | VKAVEGMAEA | CEELGIPVVS | GNVSLYNETV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EKNEIRNVFP | TPIVVGVGVL | EKAEKYTPSK | VEKESELYLV | GNLEENLRLD | GSEYLKVIHG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LIKGDVPPVD | LEKEKILINL | LISFNNKELI | TCAHDVSVGG | LLIALLEMVF | RTPYGLEVEV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YTDERPDVFF | FSENPTRVII | GVESDKAEEV | KNAVEKAGLE | WMYIGKTTEE | KKIKVTFNGD |
| 730 | 740 | ||||
| TLLEDELEEY | EKLWRTSLEK | LLGST |