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Protein

Ribose-phosphate pyrophosphokinase 1

Gene

Prps1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.

Cofactori

Enzyme regulationi

Activated by magnesium and inorganic phosphate.

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase 1 (Prps1), Ribose-phosphate pyrophosphokinase 2 (Prps2)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi128MagnesiumSequence analysis1
Metal bindingi130MagnesiumSequence analysis1
Binding sitei130ATPBy similarity1
Metal bindingi139MagnesiumSequence analysis1
Metal bindingi143MagnesiumSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi96 – 101ATPBy similarity6

GO - Molecular functioni

  • ADP binding Source: RGD
  • AMP binding Source: RGD
  • ATP binding Source: RGD
  • carbohydrate binding Source: RGD
  • GDP binding Source: RGD
  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • ribose phosphate diphosphokinase activity Source: RGD

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: RGD
  • AMP biosynthetic process Source: RGD
  • animal organ regeneration Source: RGD
  • hypoxanthine biosynthetic process Source: Ensembl
  • nervous system development Source: Ensembl
  • nucleoside metabolic process Source: InterPro
  • nucleotide biosynthetic process Source: RGD
  • ribose phosphate metabolic process Source: RGD
  • urate biosynthetic process Source: Ensembl

Keywordsi

Molecular functionKinase, Transferase
Biological processNucleotide biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-73843. 5-Phosphoribose 1-diphosphate biosynthesis.
SABIO-RKiP60892.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 1 (EC:2.7.6.1)
Alternative name(s):
Phosphoribosyl pyrophosphate synthase I
Short name:
PRS-I
Gene namesi
Name:Prps1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi61955. Prps1.

Subcellular locationi

GO - Cellular componenti

  • protein complex Source: RGD
  • ribose phosphate diphosphokinase complex Source: RGD

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001410731 – 318Ribose-phosphate pyrophosphokinase 1Add BLAST318

Proteomic databases

PaxDbiP60892.
PRIDEiP60892.

2D gel databases

World-2DPAGEi0004:P60892.

PTM databases

iPTMnetiP60892.
PhosphoSitePlusiP60892.

Expressioni

Gene expression databases

BgeeiENSRNOG00000060262.
GenevisibleiP60892. RN.

Interactioni

Subunit structurei

Homodimer. The active form is probably a hexamer composed of 3 homodimers (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248196. 2 interactors.
IntActiP60892. 1 interactor.
STRINGi10116.ENSRNOP00000029405.

Structurei

3D structure databases

ProteinModelPortaliP60892.
SMRiP60892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 227Binding of phosphoribosylpyrophosphateSequence analysisAdd BLAST16

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1448. Eukaryota.
COG0462. LUCA.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP60892.
KOiK00948.
OMAiFGWARQD.
OrthoDBiEOG091G0ZG8.
PhylomeDBiP60892.
TreeFamiTF106366.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiView protein in InterPro
IPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
PfamiView protein in Pfam
PF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiView protein in PROSITE
PS00114. PRPP_SYNTHASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P60892-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG
60 70 80 90 100
EDVYIVQSGC GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK
110 120 130 140 150
DKSRAPISAK LVANMLSVAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPA
160 170 180 190 200
VLKWIRENIS EWRNCTIVSP DAGGAKRVTS IADRLNVDFA LIHKERKKAN
210 220 230 240 250
EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG ATRVYAILTH
260 270 280 290 300
GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI
310
RRTHNGESVS YLFSHVPL
Length:318
Mass (Da):34,834
Last modified:January 23, 2007 - v2
Checksum:i46D017E969908BA0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti163R → K in AAH88149 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17258 mRNA. Translation: AAA41963.1.
M29392 mRNA. Translation: AAA41960.1.
X16554 mRNA. Translation: CAA34555.1.
M31084
, M31078, M31079, M31080, M31082, M31083 Genomic DNA. Translation: AAA41959.1.
BC078853 mRNA. Translation: AAH78853.1.
BC088149 mRNA. Translation: AAH88149.1.
PIRiA35465. KIRTR1.
RefSeqiNP_001009694.1. NM_001009694.1.
NP_058939.1. NM_017243.2.
XP_008762879.1. XM_008764657.2.
UniGeneiRn.91470.
Rn.9761.

Genome annotation databases

EnsembliENSRNOT00000078582; ENSRNOP00000071101; ENSRNOG00000060262.
GeneIDi29562.
314140.
KEGGirno:29562.
rno:314140.
UCSCiRGD:61955. rat.

Similar proteinsi

Entry informationi

Entry nameiPRPS1_RAT
AccessioniPrimary (citable) accession number: P60892
Secondary accession number(s): P09329, Q5M8A4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 120 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families