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Reviewed, UniProtKB/Swiss-Prot P14193 (KPRS_BACSU)

Last modified November 3, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ribose-phosphate pyrophosphokinase
      Short name=RPPK
    EC=2.7.6.1
Alternative name(s):
    Phosphoribosyl pyrophosphate synthetase
      Short name=P-Rib-PP synthetase
      Short name=PRPP synthetase
Gene names
Name: prs
Ordered Locus Names: BSU00510
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00583

Cofactor

Binds 1 magnesium ion per subunit. HAMAP MF_00583

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 MF_00583

Subunit structure

Homohexamer. HAMAP MF_00583

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Ribose-phosphate pyrophosphokinase HAMAP MF_00583
PRO_0000141110

Regions

Region217 – 23014Binding of phosphoribosylpyrophosphate Potential

Sites

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

Secondary structure

1 ....................................................... 317
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14193-1 [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

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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: 2555671] [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: 7584024] [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: 9384377] [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: 10742175] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

X16518 Genomic DNA. Translation: CAA34523.1.
D26185 Genomic DNA. Translation: BAA05286.1.
AL009126 Genomic DNA. Translation: CAB11827.1.
PIRKIBSRS. S05372.
RefSeqNP_387932.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DKRX-ray2.30A/B1-317[»]
1DKUX-ray2.20A/B1-317[»]
1IBSX-ray2.80A/B1-317[»]
ModBaseSearch...

Genome annotation databases

GeneID936985.
GenomeReviewsGene locus BSU00510 in contig AL009126_GR.
KEGGbsu:BSU00510.
NMPDRfig|224308.1.peg.51.

Organism-specific databases

SubtiListBG10114. prs. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP14193.
OMANVAEIMN.

Enzyme and pathway databases

BioCycBSUB224308:BSU0051-MON.
BRENDA2.7.6.1. 150.

Family and domain databases

HAMAPMF_00583.
[Tree]
InterProIPR000842. PRib-PP_synthetase_CS.
IPR000836. PRibTrfase.
IPR005946. PRPP_kinase.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHETASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: November 3, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents