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P60892 (PRPS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase 1

EC=2.7.6.1
Alternative name(s):
Phosphoribosyl pyrophosphate synthase I
Short name=PRS-I
Gene names
Name:Prps1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. HAMAP-Rule MF_00583_B

Catalytic activity

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00583_B

Cofactor

Magnesium.

Enzyme regulation

Activated by magnesium and inorganic phosphate. HAMAP-Rule MF_00583_B

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. HAMAP-Rule MF_00583_B

Subunit structure

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

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process5-phosphoribose 1-diphosphate biosynthetic process

Inferred from direct assay PubMed 9366267. Source: RGD

AMP biosynthetic process

Inferred from direct assay PubMed 2546925. Source: RGD

hypoxanthine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from electronic annotation. Source: Ensembl

nucleotide biosynthetic process

Inferred from direct assay PubMed 9748490. Source: RGD

organ regeneration

Inferred from expression pattern Ref.1. Source: RGD

ribose phosphate metabolic process

Inferred from direct assay PubMed 1651917PubMed 9348095. Source: RGD

urate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentprotein complex

Inferred from direct assay PubMed 2546925PubMed 9348095. Source: RGD

ribose phosphate diphosphokinase complex

Inferred from direct assay PubMed 2546925. Source: RGD

   Molecular_functionADP binding

Inferred from direct assay PubMed 1651917PubMed 9348095. Source: RGD

AMP binding

Inferred from direct assay PubMed 1651917PubMed 9348095PubMed 9748490. Source: RGD

ATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GDP binding

Inferred from direct assay PubMed 1651917PubMed 9348095PubMed 9748490. Source: RGD

carbohydrate binding

Inferred from direct assay PubMed 1651917PubMed 2546925PubMed 9348095PubMed 9748490. Source: RGD

kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from direct assay PubMed 1651917PubMed 9348095PubMed 9748490. Source: RGD

protein binding

Inferred from physical interaction PubMed 9366267. Source: RGD

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

ribose phosphate diphosphokinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 318317Ribose-phosphate pyrophosphokinase 1 HAMAP-Rule MF_00583_B
PRO_0000141073

Regions

Nucleotide binding96 – 1016ATP By similarity
Region212 – 22716Binding of phosphoribosylpyrophosphate Potential

Sites

Metal binding1281Magnesium Potential
Metal binding1301Magnesium Potential
Metal binding1391Magnesium Potential
Metal binding1431Magnesium Potential
Binding site1301ATP By similarity

Experimental info

Sequence conflict1631R → K in AAH88149. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P60892 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 46D017E969908BA0

FASTA31834,834
        10         20         30         40         50         60 
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG EDVYIVQSGC 

        70         80         90        100        110        120 
GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG 

       130        140        150        160        170        180 
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLKWIRENIS EWRNCTIVSP DAGGAKRVTS 

       190        200        210        220        230        240 
IADRLNVDFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG 

       250        260        270        280        290        300 
ATRVYAILTH GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI 

       310 
RRTHNGESVS YLFSHVPL 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17258 mRNA. Translation: AAA41963.1.
M29392 mRNA. Translation: AAA41960.1.
X16554 mRNA. Translation: CAA34555.1.
M31084 expand/collapse EMBL AC list , M31078, M31079, M31080, M31082, M31083 Genomic DNA. Translation: AAA41959.1.
BC078853 mRNA. Translation: AAH78853.1.
BC088149 mRNA. Translation: AAH88149.1.
PIRKIRTR1. A35465.
RefSeqNP_001009694.1. NM_001009694.1.
NP_058939.1. NM_017243.2.
UniGeneRn.91470.
Rn.9761.

3D structure databases

ProteinModelPortalP60892.
SMRP60892. Positions 3-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248196. 2 interactions.
IntActP60892. 1 interaction.
STRING10116.ENSRNOP00000029405.

Chemistry

BindingDBP60892.

PTM databases

PhosphoSiteP60892.

2D gel databases

World-2DPAGE0004:P60892.

Proteomic databases

PaxDbP60892.
PRIDEP60892.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000029571; ENSRNOP00000029405; ENSRNOG00000025166.
ENSRNOT00000040360; ENSRNOP00000043734; ENSRNOG00000031938.
GeneID29562.
314140.
KEGGrno:29562.
rno:314140.
UCSCRGD:61955. rat.

Organism-specific databases

CTD5631.
RGD61955. Prps1.

Phylogenomic databases

eggNOGCOG0462.
GeneTreeENSGT00550000074583.
HOGENOMHOG000210451.
HOVERGENHBG001520.
InParanoidP60892.
KOK00948.
OMAHIPENIE.
OrthoDBEOG7G4QG5.
PhylomeDBP60892.
TreeFamTF106366.

Enzyme and pathway databases

SABIO-RKP60892.
UniPathwayUPA00087; UER00172.

Gene expression databases

GenevestigatorP60892.

Family and domain databases

Gene3D3.40.50.2020. 2 hits.
HAMAPMF_00583_B. RibP_PPkinase_B.
InterProIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio21886.
PROP60892.

Entry information

Entry namePRPS1_RAT
AccessionPrimary (citable) accession number: P60892
Secondary accession number(s): P09329, Q5M8A4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways