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Protein

Ribose-phosphate pyrophosphokinase 2

Gene

Prps2

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)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

  • ADP binding Source: RGD
  • AMP binding Source: RGD
  • ATP binding Source: UniProtKB
  • 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: UniProtKB

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: RGD
  • AMP biosynthetic process Source: RGD
  • nucleotide biosynthetic process Source: RGD
  • organ regeneration Source: RGD
  • 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

SABIO-RKP09330.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 2 (EC:2.7.6.1)
Alternative name(s):
Phosphoribosyl pyrophosphate synthase II
Short name:
PRS-II
Gene namesi
Name:Prps2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi3415. Prps2.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 318317Ribose-phosphate pyrophosphokinase 2PRO_0000141077Add
BLAST

Proteomic databases

PaxDbiP09330.
PRIDEiP09330.

Expressioni

Gene expression databases

GenevisibleiP09330. 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

IntActiP09330. 1 interaction.
STRINGi10116.ENSRNOP00000005615.

Structurei

3D structure databases

ProteinModelPortaliP09330.
SMRiP09330. Positions 3-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1448. Eukaryota.
COG0462. LUCA.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP09330.
KOiK00948.
OMAiRENITEW.
OrthoDBiEOG7G4QG5.
PhylomeDBiP09330.
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.

P09330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG
60 70 80 90 100
EDVYIIQSGC GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK
110 120 130 140 150
DKSRAPISAK LVANMLSVAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPA
160 170 180 190 200
VLQWIRENIT EWRNCIIVSP DAGGAKRVTS IADRLNVEFA LIHKERKKAN
210 220 230 240 250
EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG ATKVYAILTH
260 270 280 290 300
GIFSGPAISR INNAAFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI
310
RRTHNGESVS YLFSHVPL
Length:318
Mass (Da):34,813
Last modified:January 23, 2007 - v3
Checksum:iA4674F6BE6667F2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351K → N in AAA41961 (PubMed:2822704).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17259 mRNA. Translation: AAA41964.1.
M29393 mRNA. Translation: AAA41961.1.
X16555 mRNA. Translation: CAA34556.1.
PIRiB29463. KIRTR2.
RefSeqiNP_036766.1. NM_012634.1.
UniGeneiRn.11320.
Rn.163618.

Genome annotation databases

EnsembliENSRNOT00000005615; ENSRNOP00000005615; ENSRNOG00000004160.
GeneIDi24689.
KEGGirno:24689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17259 mRNA. Translation: AAA41964.1.
M29393 mRNA. Translation: AAA41961.1.
X16555 mRNA. Translation: CAA34556.1.
PIRiB29463. KIRTR2.
RefSeqiNP_036766.1. NM_012634.1.
UniGeneiRn.11320.
Rn.163618.

3D structure databases

ProteinModelPortaliP09330.
SMRiP09330. Positions 3-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09330. 1 interaction.
STRINGi10116.ENSRNOP00000005615.

Proteomic databases

PaxDbiP09330.
PRIDEiP09330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005615; ENSRNOP00000005615; ENSRNOG00000004160.
GeneIDi24689.
KEGGirno:24689.

Organism-specific databases

CTDi5634.
RGDi3415. Prps2.

Phylogenomic databases

eggNOGiKOG1448. Eukaryota.
COG0462. LUCA.
GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP09330.
KOiK00948.
OMAiRENITEW.
OrthoDBiEOG7G4QG5.
PhylomeDBiP09330.
TreeFamiTF106366.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
SABIO-RKP09330.

Miscellaneous databases

NextBioi604127.
PROiP09330.

Gene expression databases

GenevisibleiP09330. RN.

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

  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 II (PRS II)."
    Ishijima S., Taira M., Tatibana M.
    Nucleic Acids Res. 17:8859-8859(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 185-194, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.

Entry informationi

Entry nameiPRPS2_RAT
AccessioniPrimary (citable) accession number: P09330
Secondary accession number(s): Q63462
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 129 of the entry and version 3 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

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 one 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.