Q8TY09
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 |
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) |
KEGG Pathway |
mka:MK0497 |
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 Q8TY09
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8TY09-F1 | Predicted | AlphaFoldDB |
No variants for Q8TY09
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8TY09 | |||||
No associated diseases with Q8TY09
5 regional properties for Q8TY09
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PurM-like, C-terminal domain | 186 - 340 | IPR010918-1 |
| domain | PurM-like, C-terminal domain | 557 - 699 | IPR010918-2 |
| domain | PurM-like, N-terminal domain | 60 - 174 | IPR016188-1 |
| domain | PurM-like, N-terminal domain | 434 - 543 | IPR016188-2 |
| domain | Phosphoribosylformylglycinamidine synthase, linker domain | 2 - 37 | 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 |
| MTLDERDLEL | IREELGRDPN | ATERAMFENM | WSEHCAYRST | RHLLRQLPSE | ADHVIVGPGD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DAAVVAIDDE | WAVVVGIESH | NHPSYVDPYN | GAATGVGGIV | RDVLSMGAFP | IALLDPLRFG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PLDGERVPYL | VDGVVRGISD | YGNRIGVPTV | GGELEFDPSY | ERNPLVNVMC | VGIVRRSEIV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RGRADRPGDV | LVLVGARTGR | DGIGGAAFAS | EELGEESEEE | DRPAVQIGDP | FTERQLIIAI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| REAVERGLVK | GCKDLGAAGL | TCAATEMAAD | GGTGVEIDVF | KVPLREEGME | PWEIMLSESQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ERMLLVVAPE | DVDEVIEICR | KYGLEASVVG | RVTDDGYLTV | KDGDDVIARV | PAEFLADGAP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EVEWEEEPYS | YPENVDVPEP | DPEDLVRSVL | SSPNVSPALR | EWVYRQYDHE | VQGRTVVKPG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HDAAVMWLQH | EGLEDVALAL | TTDSNPRHVL | IDPKTGTEGC | VAEALRNLAT | VGAEPLCLVD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| CLNFGSPENP | RVYYQLRRSI | EGLGKAAREF | EVPVVGGNVS | LYNEHEVDGP | VNPTPVIGAV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GVIRGLDYLE | DFPREPEEGE | AVIVLGETRE | ELGGSLYLIE | YHGIKGGKVP | RVRYREERAL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| HDLLRRIARK | NMVSSVTDVS | TGGLLAAVAE | LLGPVGASLS | LSEVPNSVSR | WDFLLLSESH |
| 670 | 680 | 690 | 700 | 710 | 720 |
| GRAIVTTDRP | DDVLGAAEEA | GVPAQVVGEV | TGDGVLRISV | GPVDVSLDRE | ELEELWRSPL |
| HYLE |