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Q99ZR0 (KPRS2_STRP1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase 2
Short name=RPPK 2
EC=2.7.6.1
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 2
Short name=P-Rib-PP synthase 2
Short name=PRPP synthase 2
Gene names
Name:prs2
Ordered Locus Names:SPy_1123, M5005_Spy0845
OrganismStreptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]
Taxonomic identifier301447 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00583_B

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

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 – 326326Ribose-phosphate pyrophosphokinase 2 HAMAP-Rule MF_00583_B
PRO_0000141209

Regions

Region218 – 23114Binding of phosphoribosylpyrophosphate Potential

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q99ZR0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 43E9795E6E7462A9

FASTA32635,708
        10         20         30         40         50         60 
MTERYADKQI KLFSLTSNLP IAEKIAKAAG IPLGKMSSRQ FSNGEIMINI EETVRGDDIY 

        70         80         90        100        110        120 
IIQSTSFPVN DNLWELLIMI DACKRASANT VNIVLPYFGY SRQDRVAKPR EPITAKLVAN 

       130        140        150        160        170        180 
MLTKAGIDRV VTLDLHAVQV QGFFDIPVDN LFTVPLFAER YSKLGLSGSD VVVVSPKNSG 

       190        200        210        220        230        240 
IKRARSLAEY LDSPIAIIDY AQDDSEREQG YIIGDVSGKK AILIDDILNT GKTFAEAAKI 

       250        260        270        280        290        300 
LERSGATDTY AVASHGLFAG GAADVLETAP IKEIIVTDSV KTKNRVPENV TYLSASDLIA 

       310        320 
EAIIRIHERR PLSPLFSYQP KGKNNA

« Hide

References

[1]"Complete genome sequence of an M1 strain of Streptococcus pyogenes."
Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. expand/collapse author list , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.
Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700294 / SF370 / Serotype M1.
[2]"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events."
Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.
J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004092 Genomic DNA. Translation: AAK33998.1.
CP000017 Genomic DNA. Translation: AAZ51463.1.
RefSeqNP_269277.1. NC_002737.1.
YP_282208.1. NC_007297.1.

3D structure databases

ProteinModelPortalQ99ZR0.
SMRQ99ZR0. Positions 10-317.
ModBaseSearch...

Protein-protein interaction databases

STRING160490.SPy_1123.

Proteomic databases

PaxDbQ99ZR0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK33998; AAK33998; SPy_1123.
AAZ51463; AAZ51463; M5005_Spy0845.
GeneID3572054.
901241.
KEGGspy:SPy_1123.
spz:M5005_Spy_0845.
PATRIC19715825. VBIStrPyo79812_0977.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0462.
HOGENOMHOG000210449.
KOK00948.
OMACMELSKR.
ProtClustDBPRK02458.

Enzyme and pathway databases

BioCycSPYO160490:GJ81-928-MONOMER.
SPYO293653:GHFC-904-MONOMER.
UniPathwayUPA00087; UER00172.

Family and domain databases

HAMAPMF_00583_B. RibP_PPkinase_B.
InterProIPR000842. PRib_PP_synth_CS.
IPR000836. PRibTrfase_dom.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPRS2_STRP1
AccessionPrimary (citable) accession number: Q99ZR0
Secondary accession number(s): Q48YV9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: June 1, 2001
Last modified: May 29, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents