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P14193

- KPRS_BACSU

UniProt

P14193 - KPRS_BACSU

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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.4 Publications1 Publication

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.2 Publications

Cofactori

Binds 1 magnesium ion per subunit. Manganese is also accepted, but the activity is less than 30% of that obtained with magnesium.1 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

Vmax=108 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)1 Publication

Vmax=1900 µmol/min/mg enzyme (at pH 8.2 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 8 and 8.51 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Ribose-5-phosphate1 Publication
Binding sitei136 – 1361ATP2 Publications
Binding sitei141 – 1411ATP1 Publication
Binding sitei175 – 1751Ribose-5-phosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 453ATPUniRule annotation
Nucleotide bindingi102 – 1054ATP2 Publications
Nucleotide bindingi148 – 1492ATP1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: UniProtKB-KW
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. ribose phosphate diphosphokinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 5-phosphoribose 1-diphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. nucleotide biosynthetic process Source: UniProtKB-KW
  3. ribonucleoside monophosphate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU00510-MONOMER.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase1 Publication (EC:2.7.6.12 Publications)
Short name:
RPPK1 Publication
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphate1 Publication
Phosphoribosyl diphosphate synthase2 Publications
Phosphoribosyl pyrophosphate synthase1 Publication
Short name:
P-Rib-PP synthase1 Publication
Short name:
PPRibP synthase1 Publication
Short name:
PRPP synthase1 Publication
Short name:
PRPPase1 Publication
Gene namesi
Name:prs1 Publication
Ordered Locus Names:BSU00510
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU00510. [Micado]

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981K → 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 Publication
Mutagenesisi200 – 2001R → 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 Publication
Mutagenesisi202 – 2021R → A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication
Mutagenesisi204 – 2041N → A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication
Mutagenesisi207 – 2071E → A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 317316Ribose-phosphate pyrophosphokinasePRO_0000141110Add
BLAST

Proteomic databases

PaxDbiP14193.

Interactioni

Subunit structurei

Homohexamer or homooctamer.3 Publications

Protein-protein interaction databases

IntActiP14193. 2 interactions.
MINTiMINT-8366005.
STRINGi224308.BSU00510.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145
Helixi19 – 2911
Beta strandi36 – 405
Beta strandi42 – 443
Beta strandi46 – 505
Beta strandi58 – 625
Helixi69 – 8517
Beta strandi89 – 979
Turni99 – 1024
Helixi114 – 12512
Beta strandi129 – 1346
Helixi138 – 1436
Beta strandi148 – 1514
Helixi154 – 1629
Turni163 – 1653
Beta strandi168 – 1758
Helixi176 – 1783
Helixi179 – 18810
Beta strandi193 – 1975
Beta strandi210 – 2134
Beta strandi219 – 2235
Beta strandi225 – 2295
Helixi231 – 24212
Beta strandi246 – 2516
Beta strandi253 – 2553
Helixi261 – 2666
Beta strandi268 – 2769
Beta strandi288 – 2936
Helixi296 – 30813
Helixi313 – 3153

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DKRX-ray2.30A/B1-317[»]
1DKUX-ray2.20A/B1-317[»]
1IBSX-ray2.80A/B1-317[»]
ProteinModelPortaliP14193.
SMRiP14193. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14193.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2003Ribose-5-phosphate bindingUniRule annotation
Regioni224 – 2329Ribose-5-phosphate binding2 PublicationsCurated
Regioni310 – 3123Ribose-5-phosphate binding2 Publications

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0462.
HOGENOMiHOG000210451.
InParanoidiP14193.
KOiK00948.
OMAiVNEHLME.
OrthoDBiEOG6Z99XQ.
PhylomeDBiP14193.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
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:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

EnsemblBacteriaiCAB11827; CAB11827; BSU00510.
GeneIDi936985.
KEGGibsu:BSU00510.
PATRICi18971573. VBIBacSub10457_0052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16518 Genomic DNA. Translation: CAA34523.1 .
D26185 Genomic DNA. Translation: BAA05286.1 .
AL009126 Genomic DNA. Translation: CAB11827.1 .
PIRi S05372. KIBSRS.
RefSeqi NP_387932.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DKR X-ray 2.30 A/B 1-317 [» ]
1DKU X-ray 2.20 A/B 1-317 [» ]
1IBS X-ray 2.80 A/B 1-317 [» ]
ProteinModelPortali P14193.
SMRi P14193. Positions 2-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P14193. 2 interactions.
MINTi MINT-8366005.
STRINGi 224308.BSU00510.

Proteomic databases

PaxDbi P14193.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB11827 ; CAB11827 ; BSU00510 .
GeneIDi 936985.
KEGGi bsu:BSU00510.
PATRICi 18971573. VBIBacSub10457_0052.

Organism-specific databases

GenoListi BSU00510. [Micado ]

Phylogenomic databases

eggNOGi COG0462.
HOGENOMi HOG000210451.
InParanoidi P14193.
KOi K00948.
OMAi VNEHLME.
OrthoDBi EOG6Z99XQ.
PhylomeDBi P14193.

Enzyme and pathway databases

UniPathwayi UPA00087 ; UER00172 .
BioCyci BSUB:BSU00510-MONOMER.

Miscellaneous databases

EvolutionaryTracei P14193.

Family and domain databases

Gene3Di 3.40.50.2020. 2 hits.
HAMAPi MF_00583_B. RibP_PPkinase_B.
InterProi IPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view ]
Pfami PF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53271. SSF53271. 1 hit.
TIGRFAMsi TIGR01251. ribP_PPkin. 1 hit.
PROSITEi PS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the tms and prs genes of Bacillus subtilis."
    Nilsson D., Hove-Jensen B., Arnvig K.
    Mol. Gen. Genet. 218:565-571(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
    Ogasawara N., Nakai S., Yoshikawa H.
    DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis."
    Arnvig K., Hove-Jensen B., Switzer R.L.
    Eur. J. Biochem. 192:195-200(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
  5. "Phosphoribosylpyrophosphate synthetase of Bacillus subtilis. Cloning, characterization and chromosomal mapping of the prs gene."
    Nilsson D., Hove-Jensen B.
    Gene 53:247-255(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NOMENCLATURE.
  6. "Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. Alanine-scanning mutagenesis of the flexible catalytic loop."
    Hove-Jensen B., Bentsen A.K., Harlow K.W.
    FEBS J. 272:3631-3639(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-198; ARG-200; ARG-202; ASN-204 AND GLU-207, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  7. "Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase."
    Eriksen T.A., Kadziola A., Bentsen A.-K., Harlow K.W., Larsen S.
    Nat. Struct. Biol. 7:303-308(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, SUBUNIT, ENZYME REGULATION.
  8. "Binding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis."
    Eriksen T.A., Kadziola A., Larsen S.
    Protein Sci. 11:271-279(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, SUBUNIT, ENZYME REGULATION.

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: October 29, 2014
This is version 124 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

External Data

Dasty 3