Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281MagnesiumSequence Analysis
Metal bindingi130 – 1301MagnesiumSequence Analysis
Binding sitei130 – 1301ATPBy similarity
Metal bindingi139 – 1391MagnesiumSequence Analysis
Metal bindingi143 – 1431MagnesiumSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 1016ATPBy similarity

GO - Molecular functioni

  1. ADP binding Source: RGD
  2. AMP binding Source: RGD
  3. ATP binding Source: UniProtKB
  4. carbohydrate binding Source: RGD
  5. GDP binding Source: RGD
  6. kinase activity Source: UniProtKB-KW
  7. magnesium ion binding Source: RGD
  8. protein homodimerization activity Source: UniProtKB
  9. ribose phosphate diphosphokinase activity Source: UniProtKB

GO - Biological processi

  1. 5-phosphoribose 1-diphosphate biosynthetic process Source: RGD
  2. AMP biosynthetic process Source: RGD
  3. nucleotide biosynthetic process Source: RGD
  4. organ regeneration Source: RGD
  5. ribose phosphate metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_339889. 5-Phosphoribose 1-diphosphate biosynthesis.
SABIO-RKP60892.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componentsi: Chromosome 3, Chromosome 6

Organism-specific databases

RGDi61955. Prps1.

Subcellular locationi

GO - Cellular componenti

  1. protein complex Source: RGD
  2. ribose phosphate diphosphokinase complex Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 318317Ribose-phosphate pyrophosphokinase 1PRO_0000141073Add
BLAST

Proteomic databases

PaxDbiP60892.
PRIDEiP60892.

2D gel databases

World-2DPAGE0004:P60892.

PTM databases

PhosphoSiteiP60892.

Expressioni

Gene expression databases

GenevestigatoriP60892.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi248196. 2 interactions.
IntActiP60892. 1 interaction.
STRINGi10116.ENSRNOP00000029405.

Structurei

3D structure databases

ProteinModelPortaliP60892.
SMRiP60892. Positions 3-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni212 – 22716Binding of phosphoribosylpyrophosphateSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0462.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP60892.
KOiK00948.
OMAiLCLAAQH.
OrthoDBiEOG7G4QG5.
PhylomeDBiP60892.
TreeFamiTF106366.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631R → K in AAH88149 (PubMed:15489334).Curated

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_008764657.1.
UniGeneiRn.91470.
Rn.9761.

Genome annotation databases

EnsembliENSRNOT00000029571; ENSRNOP00000029405; ENSRNOG00000025166.
GeneIDi29562.
314140.
KEGGirno:29562.
rno:314140.
UCSCiRGD:61955. rat.

Cross-referencesi

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_008764657.1.
UniGeneiRn.91470.
Rn.9761.

3D structure databases

ProteinModelPortaliP60892.
SMRiP60892. Positions 3-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248196. 2 interactions.
IntActiP60892. 1 interaction.
STRINGi10116.ENSRNOP00000029405.

Chemistry

BindingDBiP60892.

PTM databases

PhosphoSiteiP60892.

2D gel databases

World-2DPAGE0004:P60892.

Proteomic databases

PaxDbiP60892.
PRIDEiP60892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000029571; ENSRNOP00000029405; ENSRNOG00000025166.
GeneIDi29562.
314140.
KEGGirno:29562.
rno:314140.
UCSCiRGD:61955. rat.

Organism-specific databases

CTDi5631.
RGDi61955. Prps1.

Phylogenomic databases

eggNOGiCOG0462.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP60892.
KOiK00948.
OMAiLCLAAQH.
OrthoDBiEOG7G4QG5.
PhylomeDBiP60892.
TreeFamiTF106366.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
ReactomeiREACT_339889. 5-Phosphoribose 1-diphosphate biosynthesis.
SABIO-RKP60892.

Miscellaneous databases

NextBioi21886.
PROiP60892.

Gene expression databases

GenevestigatoriP60892.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and deduced amino acid sequences of two distinct cDNAs for rat phosphoribosylpyrophosphate synthetase."
    Taira M., Ishijima S., Kita K., Yamada K., Iizasa T., Tatibana M.
    J. Biol. Chem. 262:14867-14870(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Complete cDNA sequence of rat phosphoribosylpyrophosphate synthetase subunit I (PRS I)."
    Ishijima S., Taira M., Tatibana M.
    Nucleic Acids Res. 17:8860-8860(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structure of the rat PRPS1 gene encoding phosphoribosylpyrophosphate synthetase subunit I."
    Shimada H., Taira M., Yamada K., Iizasa T., Tatibana M.
    J. Biol. Chem. 265:3956-3960(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart and Thymus.
  5. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 85-96, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.

Entry informationi

Entry nameiPRPS1_RAT
AccessioniPrimary (citable) accession number: P60892
Secondary accession number(s): P09329, Q5M8A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 102 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.