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P14193 (KPRS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase

Short name=RPPK
EC=2.7.6.1
Alternative name(s):
Phosphoribosyl pyrophosphate synthase
Short name=P-Rib-PP synthase
Short name=PRPP synthase
Gene names
Name:prs
Ordered Locus Names:BSU00510
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00583_B

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. HAMAP-Rule MF_00583_B

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00583_B.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Ribose-phosphate pyrophosphokinase HAMAP-Rule MF_00583_B
PRO_0000141110

Regions

Region217 – 23014Binding of phosphoribosylpyrophosphate Potential

Sites

Metal binding1341Magnesium Potential
Metal binding1361Magnesium Potential
Metal binding1451Magnesium Potential
Metal binding1491Magnesium Potential

Secondary structure

.......................................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14193 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 0D37FC81668111EB

FASTA31734,868
        10         20         30         40         50         60 
MSNQYGDKNL KIFSLNSNPE LAKEIADIVG VQLGKCSVTR FSDGEVQINI EESIRGCDCY 

        70         80         90        100        110        120 
IIQSTSDPVN EHIMELLIMV DALKRASAKT INIVIPYYGY ARQDRKARSR EPITAKLFAN 

       130        140        150        160        170        180 
LLETAGATRV IALDLHAPQI QGFFDIPIDH LMGVPILGEY FEGKNLEDIV IVSPDHGGVT 

       190        200        210        220        230        240 
RARKLADRLK APIAIIDKRR PRPNVAEVMN IVGNIEGKTA ILIDDIIDTA GTITLAANAL 

       250        260        270        280        290        300 
VENGAKEVYA CCTHPVLSGP AVERINNSTI KELVVTNSIK LPEEKKIERF KQLSVGPLLA 

       310 
EAIIRVHEQQ SVSYLFS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16518 Genomic DNA. Translation: CAA34523.1.
D26185 Genomic DNA. Translation: BAA05286.1.
AL009126 Genomic DNA. Translation: CAB11827.1.
PIRKIBSRS. S05372.
RefSeqNP_387932.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DKRX-ray2.30A/B1-317[»]
1DKUX-ray2.20A/B1-317[»]
1IBSX-ray2.80A/B1-317[»]
ProteinModelPortalP14193.
SMRP14193. Positions 2-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP14193. 2 interactions.
MINTMINT-8366005.
STRING224308.BSU00510.

Proteomic databases

PaxDbP14193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11827; CAB11827; BSU00510.
GeneID936985.
KEGGbsu:BSU00510.
PATRIC18971573. VBIBacSub10457_0052.

Organism-specific databases

GenoListBSU00510. [Micado]

Phylogenomic databases

eggNOGCOG0462.
HOGENOMHOG000210451.
KOK00948.
OMAYVQIQES.
OrthoDBEOG6Z99XQ.
ProtClustDBPRK01259.

Enzyme and pathway databases

BioCycBSUB:BSU00510-MONOMER.
UniPathwayUPA00087; UER00172.

Family and domain databases

HAMAPMF_00583_B. RibP_PPkinase_B.
InterProIPR000842. PRib_PP_synth_CS.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamPF14572. Pribosyl_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14193.

Entry information

Entry nameKPRS_BACSU
AccessionPrimary (citable) accession number: P14193
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: February 19, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

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