Q9X0X7
Gene name |
purD |
Protein name |
Phosphoribosylamine--glycine ligase |
Names |
GARS, Glycinamide ribonucleotide synthetase, Phosphoribosylglycinamide synthetase |
Species |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
KEGG Pathway |
tma:TM1250 |
EC number |
6.3.4.13: Other carbon--nitrogen ligases |
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
2 structures for Q9X0X7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1VKZ | X-ray | 230 A | A/B | 1-400 | PDB |
| AF-Q9X0X7-F1 | Predicted | AlphaFoldDB |
No variants for Q9X0X7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9X0X7 | |||||
No associated diseases with Q9X0X7
5 regional properties for Q9X0X7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ATP-grasp fold | 99 - 303 | IPR011761 |
| conserved_site | Phosphoribosylglycinamide synthetase, conserved site | 277 - 284 | IPR020559 |
| domain | Phosphoribosylglycinamide synthetase, C-domain | 315 - 400 | IPR020560 |
| domain | Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain | 93 - 283 | IPR020561 |
| domain | Phosphoribosylglycinamide synthetase, N-terminal | 5 - 92 | IPR020562 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.4.13 | Other carbon--nitrogen ligases |
| 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. |
| metal ion binding | Binding to a metal ion. |
| phosphoribosylamine-glycine ligase activity | Catalysis of the reaction: 5-phospho-D-ribosylamine + ATP + glycine = N(1)-(5-phospho-D-ribosyl)glycinamide + ADP + 2 H(+) + phosphate. |
2 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. |
| purine nucleobase biosynthetic process | The chemical reactions and pathways resulting in the formation of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKAVRVHILG | SGGREHAIGW | AFAKQGYEVH | FYPGNAGTKR | DGTNHPYEGE | KTLKAIPEED |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IVIPGSEEFL | VEGVSNWRSN | VFGPVKEVAR | LEGSKVYAKR | FMKKYGIRTA | RFEVAETPEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LREKIKKFSP | PYVIKADGLA | RGKGVLILDS | KEETIEKGSK | LIIGELIKGV | KGPVVIDEFL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AGNELSAMAV | VNGRNFVILP | FVRDYKRLMD | GDRGPNTGGM | GSWGPVEIPS | DTIKKIEELF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DKTLWGVEKE | GYAYRGFLYL | GLMLHDGDPY | ILEYNVRLGD | PETEVIVTLN | PEGFVNAVLE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GYRGGKMEPV | EPRGFAVDVV | LAARGYPDAP | EKGKEITLPE | EGLIFFAGVA | EKDGKLVTNG |
| 370 | 380 | 390 | |||
| GRVLHCMGTG | ETKEEARRKA | YELAEKVHFE | GKTYRRDIAL |