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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. It can also use dATP as diphosphoryl donor.UniRule annotation1 Publication

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 PublicationNote: Binds 1 Mg2+ ion per subunit. Mn2+ is also accepted, but the activity is less than 15% of that obtained with Mg2+, when assayed at pH 9.5.UniRule annotation1 Publication

Enzyme regulationi

Activated by phosphate ion. Maximal activity is obtained at 190 mM, with a fairly flat activity profile around this concentration. Further increase in phosphate ion concentration inhibited the activity of the enzyme. Thus, at 250 mM the activity is 80% of maximal activity. Inhibited by alpha,beta-methylene ATP and ADP.1 Publication

Kineticsi

  1. KM=2.6 mM for ATP (at pH 9 and 85 degrees Celsius)1 Publication
  2. KM=2.8 mM for ribose 5-phosphate (at pH 9 and 85 degrees Celsius)1 Publication
  1. Vmax=2.2 mmol/min/mg enzyme (at pH 9 and 85 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.5. The activity declines strongly above pH 10.1 Publication

Temperature dependencei

Optimum temperature is 85 degrees Celsius. 70% of maximal activity at 72 and 95 degrees Celsius.1 Publication

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 annotation1 Publication
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931ATPUniRule annotation1 Publication
Metal bindingi123 – 1231MagnesiumUniRule annotation
Metal bindingi125 – 1251MagnesiumUniRule annotation
Binding sitei125 – 1251ATPUniRule annotation1 Publication
Binding sitei163 – 1631Ribose-5-phosphateUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 363ATPUniRule annotation1 Publication
Nucleotide bindingi92 – 954ATP1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.6.1. 3260.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase1 PublicationUniRule annotation (EC:2.7.6.1UniRule annotation1 Publication)
Short name:
RPPK1 PublicationUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphateUniRule annotation
Phosphoribosyl diphosphate synthase1 PublicationUniRule annotation
Phosphoribosyl pyrophosphate synthase1 PublicationUniRule annotation
Short name:
P-Rib-PP synthaseUniRule annotation
Short name:
PRPP synthase1 PublicationUniRule annotation
Short name:
PRPPaseUniRule annotation
Gene namesi
Name:prs1 PublicationUniRule annotation
Ordered Locus Names:MJ1366
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Ribose-phosphate pyrophosphokinasePRO_0000141238Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_1366.

Structurei

Secondary structure

1
284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi7 – 93Combined sources
Helixi10 – 1910Combined sources
Beta strandi27 – 315Combined sources
Beta strandi37 – 415Combined sources
Beta strandi47 – 537Combined sources
Helixi59 – 7416Combined sources
Turni75 – 773Combined sources
Beta strandi80 – 845Combined sources
Turni89 – 924Combined sources
Helixi104 – 11512Combined sources
Beta strandi117 – 1237Combined sources
Helixi127 – 1326Combined sources
Beta strandi137 – 1404Combined sources
Helixi143 – 1508Combined sources
Turni151 – 1533Combined sources
Beta strandi158 – 1636Combined sources
Helixi164 – 1663Combined sources
Helixi167 – 17711Combined sources
Beta strandi181 – 1844Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi216 – 2183Combined sources
Helixi219 – 23012Combined sources
Beta strandi235 – 2428Combined sources
Helixi249 – 2568Combined sources
Beta strandi259 – 2646Combined sources
Beta strandi272 – 2743Combined sources
Helixi277 – 2815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U9YX-ray2.65A/B/C/D1-284[»]
1U9ZX-ray2.80A/B/C/D1-284[»]
ProteinModelPortaliQ58761.
SMRiQ58761. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58761.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 1883Ribose-5-phosphate bindingUniRule annotation
Regioni212 – 2209Ribose-5-phosphate bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00067. Archaea.
COG0462. LUCA.
InParanoidiQ58761.
KOiK00948.
OMAiITINPHE.
PhylomeDBiQ58761.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_A. RibP_PPkinase_A. 1 hit.
InterProiIPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 2 hits.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.

Sequencei

Sequence statusi: Complete.

Q58761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVVSGSQSQ NLAFKVAKLL NTKLTRVEYK RFPDNEIYVR IVDEINDDEA
60 70 80 90 100
VIINTQKNQN DAIVETILLC DALRDEGVKK ITLVAPYLAY ARQDKKFNPG
110 120 130 140 150
EAISIRALAK IYSNIVDKLI TINPHETHIK DFFTIPFIYG DAVPKLAEYV
160 170 180 190 200
KDKLNDPIVL APDKGALEFA KTASKILNAE YDYLEKTRLS PTEIQIAPKT
210 220 230 240 250
LDAKDRDVFI VDDIISTGGT MATAVKLLKE QGAKKIIAAC VHPVLIGDAL
260 270 280
NKLYSAGVEE VVGTDTYLSE VSKVSVAEVI VDLL
Length:284
Mass (Da):31,395
Last modified:October 25, 2002 - v2
Checksum:i9EAE9805785B1127
GO

Sequence cautioni

The sequence AAB99374 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99374.1. Different initiation.
PIRiE64470.

Genome annotation databases

EnsemblBacteriaiAAB99374; AAB99374; MJ_1366.
KEGGimja:MJ_1366.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99374.1. Different initiation.
PIRiE64470.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U9YX-ray2.65A/B/C/D1-284[»]
1U9ZX-ray2.80A/B/C/D1-284[»]
ProteinModelPortaliQ58761.
SMRiQ58761. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99374; AAB99374; MJ_1366.
KEGGimja:MJ_1366.

Phylogenomic databases

eggNOGiarCOG00067. Archaea.
COG0462. LUCA.
InParanoidiQ58761.
KOiK00948.
OMAiITINPHE.
PhylomeDBiQ58761.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BRENDAi2.7.6.1. 3260.

Miscellaneous databases

EvolutionaryTraceiQ58761.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_A. RibP_PPkinase_A. 1 hit.
InterProiIPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 2 hits.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKPRS_METJA
AccessioniPrimary (citable) accession number: Q58761
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 25, 2002
Last modified: September 7, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

M.jannaschii PRPP synthase is more compact than the PRPP synthase in the B. subtilis subunit. This is mainly due to truncations of eight residues at the N terminus, 14 residues at the C terminus and to a seven-residue shorter loop.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.