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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
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 sitei108Ribose-5-phosphateUniRule annotation1
Metal bindingi132MagnesiumUniRule annotation1
Metal bindingi134MagnesiumUniRule annotation1
Binding sitei134ATPUniRule annotation1
Binding sitei139ATPUniRule annotation1
Metal bindingi143MagnesiumUniRule annotation1
Metal bindingi147MagnesiumUniRule annotation1
Binding sitei173Ribose-5-phosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi40 – 42ATPUniRule annotation3
Nucleotide bindingi99 – 102ATPUniRule annotation4

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
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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Proteomic databases

PRIDEiP65234.

Structurei

3D structure databases

ProteinModelPortaliP65234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni196 – 198Ribose-5-phosphate bindingUniRule annotation3
Regioni223 – 230Ribose-5-phosphate bindingUniRule annotation8
Regioni310 – 312Ribose-5-phosphate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000210449.
KOiK00948.
OMAiHENVRGQ.

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.

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.
PATRICi20363118. VBINeiMen132687_1264.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP65234.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP65234.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM08304; CAM08304; NMA1093.
KEGGinma:NMA1093.
PATRICi20363118. VBINeiMen132687_1264.

Phylogenomic databases

HOGENOMiHOG000210449.
KOiK00948.
OMAiHENVRGQ.

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_NEIMA
AccessioniPrimary (citable) accession number: P65234
Secondary accession number(s): A1IRB8, Q9JQV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 85 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.