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
Bacillus subtilis (strain 168)
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.UniRule annotation1 Publication4 Publications

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation1 Publication, Mn2+UniRule annotation1 PublicationNote: Binds 1 Mg2+ ion per subunit. Mn2+ is also accepted, but the activity is less than 30% of that obtained with Mg2+.UniRule annotation1 Publication

Enzyme regulationi

Activated by phosphate and sulfate ions. Allosterically inhibited by alpha,beta-methylene ATP (mADP) and ADP. GDP, GMP and UTP are a weak inhibitors.4 Publications

Kineticsi

  1. KM=191 µM for ATP (at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=230 µM for Rib-5-P (at pH 8 and 37 degrees Celsius)1 Publication
  3. KM=480 µM for Rib-5-P (at pH 8.2 and 37 degrees Celsius)1 Publication
  4. KM=660 µM for ATP (at pH 8.2 and 37 degrees Celsius)1 Publication
  1. Vmax=108 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)1 Publication
  2. Vmax=1900 µmol/min/mg enzyme (at pH 8.2 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 8 and 8.5.1 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 annotation2 Publications
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 sitei110Ribose-5-phosphateUniRule annotation1 Publication1
Metal bindingi134MagnesiumUniRule annotation1
Metal bindingi136MagnesiumUniRule annotation1
Binding sitei136ATPUniRule annotation2 Publications1
Binding sitei141ATPUniRule annotation1 Publication1
Metal bindingi145MagnesiumUniRule annotation1
Metal bindingi149MagnesiumUniRule annotation1
Binding sitei175Ribose-5-phosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi43 – 45ATPUniRule annotation3
Nucleotide bindingi102 – 105ATPUniRule annotation2 Publications4
Nucleotide bindingi149 – 150ATPUniRule annotation1 Publication2

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

BioCyciBSUB:BSU00510-MONOMER.
SABIO-RKP14193.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase1 PublicationUniRule annotation (EC:2.7.6.1UniRule annotation2 Publications)
Short name:
RPPK1 PublicationUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphate1 PublicationUniRule annotation
Phosphoribosyl diphosphate synthase2 PublicationsUniRule annotation
Phosphoribosyl pyrophosphate synthase1 PublicationUniRule annotation
Short name:
P-Rib-PP synthase1 PublicationUniRule annotation
Short name:
PPRibP synthase1 Publication
Short name:
PRPP synthase1 PublicationUniRule annotation
Short name:
PRPPase1 PublicationUniRule annotation
Gene namesi
Name:prs1 PublicationUniRule annotation
Ordered Locus Names:BSU00510
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi198K → A: Strong decrease of the Vmax value compared to that of the wild-type. The affinity binding for ATP and Rib-5-P are slightly altered compared to the wild-type. The cooperativity of ADP binding is reduced. 1 Publication1
Mutagenesisi200R → A: Strong decrease of the Vmax value compared to that of the wild-type enzyme. The affinity binding for ATP and Rib-5-P are slightly altered compared to the wild-type. 1 Publication1
Mutagenesisi202R → A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication1
Mutagenesisi204N → A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication1
Mutagenesisi207E → A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001411102 – 317Ribose-phosphate pyrophosphokinaseAdd BLAST316

Proteomic databases

PaxDbiP14193.

Interactioni

Subunit structurei

Homohexamer or homooctamer.3 Publications

Protein-protein interaction databases

IntActiP14193. 2 interactors.
MINTiMINT-8366005.
STRINGi224308.Bsubs1_010100000260.

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 14Combined sources5
Helixi19 – 29Combined sources11
Beta strandi36 – 40Combined sources5
Beta strandi42 – 44Combined sources3
Beta strandi46 – 50Combined sources5
Beta strandi58 – 62Combined sources5
Helixi69 – 85Combined sources17
Beta strandi89 – 97Combined sources9
Turni99 – 102Combined sources4
Helixi114 – 125Combined sources12
Beta strandi129 – 134Combined sources6
Helixi138 – 143Combined sources6
Beta strandi148 – 151Combined sources4
Helixi154 – 162Combined sources9
Turni163 – 165Combined sources3
Beta strandi168 – 175Combined sources8
Helixi176 – 178Combined sources3
Helixi179 – 188Combined sources10
Beta strandi193 – 197Combined sources5
Beta strandi210 – 213Combined sources4
Beta strandi219 – 223Combined sources5
Beta strandi225 – 229Combined sources5
Helixi231 – 242Combined sources12
Beta strandi246 – 251Combined sources6
Beta strandi253 – 255Combined sources3
Helixi261 – 266Combined sources6
Beta strandi268 – 276Combined sources9
Beta strandi288 – 293Combined sources6
Helixi296 – 308Combined sources13
Helixi313 – 315Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DKRX-ray2.30A/B1-317[»]
1DKUX-ray2.20A/B1-317[»]
1IBSX-ray2.80A/B1-317[»]
ProteinModelPortaliP14193.
SMRiP14193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14193.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni198 – 200Ribose-5-phosphate bindingUniRule annotation3
Regioni225 – 232Ribose-5-phosphate bindingUniRule annotationCurated2 Publications8
Regioni311 – 313Ribose-5-phosphate bindingUniRule annotation2 Publications3

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210451.
InParanoidiP14193.
KOiK00948.
OMAiDGEIMVE.
PhylomeDBiP14193.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNQYGDKNL KIFSLNSNPE LAKEIADIVG VQLGKCSVTR FSDGEVQINI
60 70 80 90 100
EESIRGCDCY IIQSTSDPVN EHIMELLIMV DALKRASAKT INIVIPYYGY
110 120 130 140 150
ARQDRKARSR EPITAKLFAN LLETAGATRV IALDLHAPQI QGFFDIPIDH
160 170 180 190 200
LMGVPILGEY FEGKNLEDIV IVSPDHGGVT RARKLADRLK APIAIIDKRR
210 220 230 240 250
PRPNVAEVMN IVGNIEGKTA ILIDDIIDTA GTITLAANAL VENGAKEVYA
260 270 280 290 300
CCTHPVLSGP AVERINNSTI KELVVTNSIK LPEEKKIERF KQLSVGPLLA
310
EAIIRVHEQQ SVSYLFS
Length:317
Mass (Da):34,868
Last modified:January 1, 1990 - v1
Checksum:i0D37FC81668111EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16518 Genomic DNA. Translation: CAA34523.1.
D26185 Genomic DNA. Translation: BAA05286.1.
AL009126 Genomic DNA. Translation: CAB11827.1.
PIRiS05372. KIBSRS.
RefSeqiNP_387932.1. NC_000964.3.
WP_003218353.1. NZ_JNCM01000028.1.

Genome annotation databases

EnsemblBacteriaiCAB11827; CAB11827; BSU00510.
GeneIDi11237812.
936985.
KEGGibsu:BSU00510.
PATRICi18971573. VBIBacSub10457_0052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16518 Genomic DNA. Translation: CAA34523.1.
D26185 Genomic DNA. Translation: BAA05286.1.
AL009126 Genomic DNA. Translation: CAB11827.1.
PIRiS05372. KIBSRS.
RefSeqiNP_387932.1. NC_000964.3.
WP_003218353.1. NZ_JNCM01000028.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DKRX-ray2.30A/B1-317[»]
1DKUX-ray2.20A/B1-317[»]
1IBSX-ray2.80A/B1-317[»]
ProteinModelPortaliP14193.
SMRiP14193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14193. 2 interactors.
MINTiMINT-8366005.
STRINGi224308.Bsubs1_010100000260.

Proteomic databases

PaxDbiP14193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11827; CAB11827; BSU00510.
GeneIDi11237812.
936985.
KEGGibsu:BSU00510.
PATRICi18971573. VBIBacSub10457_0052.

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210451.
InParanoidiP14193.
KOiK00948.
OMAiDGEIMVE.
PhylomeDBiP14193.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciBSUB:BSU00510-MONOMER.
SABIO-RKP14193.

Miscellaneous databases

EvolutionaryTraceiP14193.

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_BACSU
AccessioniPrimary (citable) accession number: P14193
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 137 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.