P46585
Gene name |
PRS1 |
Protein name |
Ribose-phosphate pyrophosphokinase 1 |
Names |
Phosphoribosyl pyrophosphate synthase 1 |
Species |
Candida albicans (Yeast) |
KEGG Pathway |
|
EC number |
2.7.6.1: Diphosphotransferases |
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 P46585
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P46585-F1 | Predicted | AlphaFoldDB |
No variants for P46585
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P46585 | |||||
No associated diseases with P46585
3 regional properties for P46585
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.6.1 | Diphosphotransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| ribose phosphate diphosphokinase complex | A protein complex having ribose phosphate diphosphokinase activity. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| ribose phosphate diphosphokinase activity | Catalysis of the reaction: D-ribose 5-phosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + 2 H(+). |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| 5-phosphoribose 1-diphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate. |
| fungal-type cell wall organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall. |
| nucleotide biosynthetic process | The chemical reactions and pathways resulting in the formation of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates). |
| phosphorylation | The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. |
| ribonucleoside monophosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of a ribonucleoside monophosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with phosphate on the sugar. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTNSIKLLA | SDVHRGLAEL | VSKRLGLRLT | PSELKRESTG | EVQFSIGESV | RDEDIFIICQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IGSGEVNDRV | FELMIMINAC | KTASARRITV | ILPNFPYARQ | DRKDKSRAPI | TAKLMADMLT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TAGCDHVITM | DLHASQIQGF | FDVPVDNLYA | EPSVVRYIKE | TIDYSEAIII | SSDAGGAKRA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AGLADRLDLN | FELIHKERAR | ANEVSRMVLV | VDVTDKICVI | VDDMADTCGT | LAKAAEVLLD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NNAKDVIAIV | THGILSGNAI | KNINNSKLKK | VVCTNTVPFE | DKLKLCLKLD | TIDISAVIAE |
| 310 | 320 | ||||
| SIRRLHNGES | ISYLFKNAPC | K |