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Reviewed, UniProtKB/Swiss-Prot Q8NRU9 (KPRS_CORGL)

Last modified November 3, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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
Synonyms: prsA
Ordered Locus Names: Cgl0942, cg1075
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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 By similarity.

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Ribose-phosphate pyrophosphokinase HAMAP MF_00583
PRO_0000141131

Regions

Region223 – 23614Binding of phosphoribosylpyrophosphate Potential

Sites

Metal binding1361Magnesium Potential
Metal binding1381Magnesium Potential
Metal binding1471Magnesium Potential
Metal binding1511Magnesium Potential

Sequences

Sequence LengthMass (Da)Tools
Q8NRU9-1 [UniParc].

Last modified October 25, 2002. Version 1.
Checksum: D1FD1944CCD9E77A

FASTA32535,551
        10         20         30         40         50         60 
MTAHWKQNQK NLMLFSGRAH PELAEAVAKE LDVNVTPMTA RDFANGEIYV RFEESVRGSD 

        70         80         90        100        110        120 
CFVLQSHTQP LNKWLMEQLL MIDALKRGSA KRITAILPFY PYARQDKKHR GREPISARLI 

       130        140        150        160        170        180 
ADLMLTAGAD RIVSVDLHTD QIQGFFDGPV DHMHAMPILT DHIKENYNLD NICVVSPDAG 

       190        200        210        220        230        240 
RVKVAEKWAN TLGDAPMAFV HKTRSTEVAN QVVANRVVGD VDGKDCVLLD DMIDTGGTIA 

       250        260        270        280        290        300 
GAVGVLKKAG AKSVVIACTH GVFSDPARER LSACGAEEVI TTDTLPQSTE GWSNLTVLSI 

       310        320 
APLLARTINE IFENGSVTTL FEGEA 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

BA000036 Genomic DNA. Translation: BAB98335.1.
BX927150 Genomic DNA. Translation: CAF19649.1.
RefSeqNP_600170.1.
YP_225235.1.

3D structure databases

HSSPHSSP built from PDB template 1DKR based on UniProtKB P14193.
ModBaseSearch...

Genome annotation databases

GeneID1018934.
3343409.
GenomeReviewsGene locus Cgl0942 in contig BA000036_GR.
Gene locus cg1075 in contig BX927147_GR.
KEGGcgb:cg1075.
cgl:NCgl0905.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8NRU9.
OMASGRTPIS.

Enzyme and pathway databases

BioCycCGLU196627-1:CG1075-MON.
BRENDA2.7.6.1. 812.

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...

Entry information

Entry nameKPRS_CORGL
AccessionPrimary (citable) accession number: Q8NRU9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 25, 2002
Last modified: November 3, 2009
This is version 45 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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