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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of ribose 1,5-bisphosphate. Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

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).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase (prs)
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
Binding sitei111Ribose-5-phosphateUniRule annotation1
Metal bindingi135MagnesiumUniRule annotation1
Metal bindingi137MagnesiumUniRule annotation1
Binding sitei137ATPUniRule annotation1
Binding sitei142ATPUniRule annotation1
Metal bindingi146MagnesiumUniRule annotation1
Metal bindingi150MagnesiumUniRule annotation1
Binding sitei179Ribose-5-phosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 46ATPUniRule annotation3
Nucleotide bindingi103 – 106ATPUniRule annotation4
Nucleotide bindingi150 – 151ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

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

UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinaseUniRule annotation (EC:2.7.6.1UniRule annotation)
Short name:
RPPKUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphateUniRule annotation
Phosphoribosyl diphosphate synthaseUniRule annotation
Phosphoribosyl pyrophosphate synthaseUniRule annotation
Short name:
P-Rib-PP synthaseUniRule annotation
Short name:
PRPP synthaseUniRule annotation
Short name:
PRPPaseUniRule annotation
Gene namesi
Name:prsUniRule annotation
Ordered Locus Names:SAV0500
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001411871 – 321Ribose-phosphate pyrophosphokinaseAdd BLAST321

Proteomic databases

PaxDbiP65236.
PRIDEiP65236.

2D gel databases

World-2DPAGE0002:P65236.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV0500.

Structurei

3D structure databases

ProteinModelPortaliP65236.
SMRiP65236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni202 – 204Ribose-5-phosphate bindingUniRule annotation3
Regioni229 – 236Ribose-5-phosphate bindingUniRule annotation8
Regioni315 – 317Ribose-5-phosphate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210449.
KOiK00948.
OMAiDGEIMVE.
PhylomeDBiP65236.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
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.

P65236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNNEYKNSS LKIFSLKGNE ALAQEVADQV GIELGKCSVK RFSDGEIQIN
60 70 80 90 100
IEESIRGCDV FIIQPTSYPV NLHLMELLIM IDACKRASAA TINIVVPYYG
110 120 130 140 150
YARQDRKARS REPITAKLVA NLIETAGATR MIALDLHAPQ IQGFFDIPID
160 170 180 190 200
HLMGVPILAK HFKDDPNINP EECVVVSPDH GGVTRARKLA DILKTPIAII
210 220 230 240 250
DKRRPRPNVA EVMNIVGEIE GRTAIIIDDI IDTAGTITLA AQALKDKGAK
260 270 280 290 300
EVYACCTHPV LSGPAKERIE NSAIKELIVT NSIHLDEDRK PSNTKELSVA
310 320
GLIAQAIIRV YERESVSVLF D
Length:321
Mass (Da):35,284
Last modified:October 11, 2004 - v1
Checksum:i70A955AA62C9415E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB56662.1.
RefSeqiWP_000933774.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB56662; BAB56662; SAV0500.
GeneIDi28378936.
KEGGisav:SAV0500.
PATRICi19561622. VBIStaAur52173_0504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB56662.1.
RefSeqiWP_000933774.1. NC_002758.2.

3D structure databases

ProteinModelPortaliP65236.
SMRiP65236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV0500.

2D gel databases

World-2DPAGE0002:P65236.

Proteomic databases

PaxDbiP65236.
PRIDEiP65236.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB56662; BAB56662; SAV0500.
GeneIDi28378936.
KEGGisav:SAV0500.
PATRICi19561622. VBIStaAur52173_0504.

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210449.
KOiK00948.
OMAiDGEIMVE.
PhylomeDBiP65236.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
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...

Entry informationi

Entry nameiKPRS_STAAM
AccessioniPrimary (citable) accession number: P65236
Secondary accession number(s): Q99WA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete 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.