Q7V111
Gene name |
prs |
Protein name |
Ribose-phosphate pyrophosphokinase |
Names |
RPPK, 5-phospho-D-ribosyl alpha-1-diphosphate, Phosphoribosyl diphosphate synthase, Phosphoribosyl pyrophosphate synthase, P-Rib-PP synthase, PRPP synthase, PRPPase |
Species |
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4) |
KEGG Pathway |
pmm:PMM1080 |
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 Q7V111
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7V111-F1 | Predicted | AlphaFoldDB |
No variants for Q7V111
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7V111 | |||||
No associated diseases with Q7V111
1 regional properties for Q7V111
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Wnt protein, conserved site | 217 - 226 | IPR018161 |
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 |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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(+). |
4 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. |
| 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 |
| MTSFITAVDN | EEPTFNLTNS | RLRLVSGTSN | PKLAEEIASY | LGIENVPLVS | KRFADGELYV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QIQQSIRGCD | VFLIQPTCAP | VNDSLMELMI | MVDACKRASA | RQITAVIPYF | GYARADRKTS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GRESITAKLT | ANLLEKSGVD | RVLAMDLHSA | QIQGYFDIPC | DHIYGSPVLI | DYLESLKLEE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VVVVSPDVGG | VARARAFAKL | MSDAPLAIID | KRRSAHNIAE | SLTVIGEVKG | KTAILIDDMI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DTGGTICSGA | NLLKKEGAKR | IFACASHAVF | SPPSYERLSS | KDLFEQVIVT | NSIPVIDNYE |
| 310 | 320 | 330 | |||
| FPQLKVLSVA | NMLGEAIWRI | HEESSVSSMF | R |