Q0KE53
Gene name |
purC |
Protein name |
Phosphoribosylaminoimidazole-succinocarboxamide synthase |
Names |
SAICAR synthetase |
Species |
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) |
KEGG Pathway |
reh:H16_A0569 |
EC number |
6.3.2.6: Acid--amino-acid ligases (peptide synthases) |
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 Q0KE53
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0KE53-F1 | Predicted | AlphaFoldDB |
No variants for Q0KE53
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0KE53 | |||||
No associated diseases with Q0KE53
3 regional properties for Q0KE53
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | SAICAR synthetase, conserved site | 106 - 120 | IPR018236-1 |
| conserved_site | SAICAR synthetase, conserved site | 205 - 213 | IPR018236-2 |
| domain | SAICAR synthetase/ADE2, N-terminal | 13 - 298 | IPR028923 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.2.6 | Acid--amino-acid ligases (peptide synthases) |
| 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 |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| phosphoribosylaminoimidazolesuccinocarboxamide synthase activity | Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate + ATP = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + 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 |
| MSNALYQSSI | NSLPLLGHGK | VRDNYAVGND | KLLIVTTDRL | SAFDVIMGEP | IPDKGRVLNQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MANFWFRKLA | HIVPNHETGI | APETVVAPEE | VEQVKGRAVV | VKRLRPILVE | AVVRGYLAGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GWKDYQATGK | VCGIELPAGL | QNAQKLPEPI | FTPAAKAEMG | EHDENISFAE | VEARIGIALA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RQMRDISIRL | YKEAAEFAAT | RGIIIADTKF | EFGLDDNGVL | TLMDEVLTAD | SSRFWPADSY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QVGTNPPSFD | KQFVRDWLEA | VRIDGKPWPK | TAPAPQLPDE | VIEKTAAKYR | EALTRLTGEE |
| LQ |