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

Gene

prs

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 2 Mg2+ ions 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
Metal bindingi134Magnesium 1UniRule annotation1
Metal bindingi173Magnesium 2UniRule annotation1
Active sitei196UniRule annotation1
Binding sitei198Ribose-5-phosphateUniRule annotation1
Binding sitei222Ribose-5-phosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi40 – 42ATPUniRule annotation3
Nucleotide bindingi99 – 100ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processNucleotide biosynthesis
LigandATP-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
Synonyms:prsA
Ordered Locus Names:NMA1093
OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Taxonomic identifieri122587 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000626 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001411661 – 327Ribose-phosphate pyrophosphokinaseAdd BLAST327

Interactioni

Subunit structurei

Homohexamer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP65234
SMRiP65234
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni226 – 230Ribose-5-phosphate bindingUniRule annotation5

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000210449
KOiK00948
OMAiFGWARQD

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
IPR037515 Rib-P_diPkinase_bac
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.

P65234-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYDSLMVF TGNANPELAQ RVVRHLDISL GNASVSKFSD GEVAVELLEN
60 70 80 90 100
VRGRDVFILQ PTCAPTNDNL MEILTMADAL KRASAGRITT AIPYFGYARQ
110 120 130 140 150
DRRPRSVRVP ISAKLVANML YSAGIDRVLT VDLHADQIQG FFDIPVDNIY
160 170 180 190 200
ATPILLNDIK QQRIENLTVV SPDIGGVVRA RAVAKSLNAD LAIIDKRRPK
210 220 230 240 250
ANVAEVMNII GDIQGRTCLI VDDMIDTANT LCKAAVALKE RGAERVLAYA
260 270 280 290 300
SHAVFSGEAV SRIASSEIDQ VVVTDTIPLS EAAKNCDRIR QVTIAGLLAE
310 320
TVRRISNEES VSYLFNEEVM TGSMLLP
Length:327
Mass (Da):35,598
Last modified:October 11, 2004 - v1
Checksum:iB92FF8F029589B92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA Translation: CAM08304.1
RefSeqiWP_002213870.1, NC_003116.1

Genome annotation databases

EnsemblBacteriaiCAM08304; CAM08304; NMA1093
KEGGinma:NMA1093

Similar proteinsi

Entry informationi

Entry nameiKPRS_NEIMA
AccessioniPrimary (citable) accession number: P65234
Secondary accession number(s): A1IRB8, Q9JQV4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 23, 2018
This is version 91 of the entry and version 1 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health