Q6GJH1 (KPRS_STAAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	SAR0501

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule 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-Rule MF_00583
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway nucleoside metabolic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: HAMAP ribose phosphate diphosphokinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 321	321	Ribose-phosphate pyrophosphokinase HAMAP-Rule MF_00583		PRO_0000141189
Regions
	Region	221 – 234	14	Binding of phosphoribosylpyrophosphate Potential
Sites
	Metal binding	135	1	Magnesium Potential
	Metal binding	137	1	Magnesium Potential
	Metal binding	146	1	Magnesium Potential
	Metal binding	150	1	Magnesium Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6GJH1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 70A955AA62C9415E	FASTA	321	35,284
	10 20 30 40 50 60 MLNNEYKNSS LKIFSLKGNE ALAQEVADQV GIELGKCSVK RFSDGEIQIN IEESIRGCDV 70 80 90 100 110 120 FIIQPTSYPV NLHLMELLIM IDACKRASAA TINIVVPYYG YARQDRKARS REPITAKLVA 130 140 150 160 170 180 NLIETAGATR MIALDLHAPQ IQGFFDIPID HLMGVPILAK HFKDDPNINP EECVVVSPDH 190 200 210 220 230 240 GGVTRARKLA DILKTPIAII DKRRPRPNVA EVMNIVGEIE GRTAIIIDDI IDTAGTITLA 250 260 270 280 290 300 AQALKDKGAK EVYACCTHPV LSGPAKERIE NSAIKELIVT NSIHLDEDRK PSNTKELSVA 310 320 GLIAQAIIRV YERESVSVLF D

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MRSA252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571856 Genomic DNA. Translation: CAG39523.1.
RefSeq	YP_039951.1. NC_002952.2.
3D structure databases
ProteinModelPortal	Q6GJH1.
SMR	Q6GJH1. Positions 10-320.
ModBase	Search...
Protein-protein interaction databases
STRING	282458.SAR0501.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG39523; CAG39523; SAR0501.
GeneID	2860154.
KEGG	sar:SAR0501.
PATRIC	19544524. VBIStaAur71814_0508.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0462.
HOGENOM	HOG000210449.
KO	K00948.
OMA	YVQIQES.
ProtClustDB	PRK01259.
Enzyme and pathway databases
BioCyc	SAUR282458:GJA5-505-MONOMER.
UniPathway	UPA00087; UER00172.
Family and domain databases
HAMAP	MF_00583_B. RibP_PPkinase_B.
InterPro	IPR000842. PRib_PP_synth_CS. IPR000836. PRibTrfase_dom. IPR005946. Rib-P_diPkinase. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. ribP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPRS_STAAR

Accession

Primary (citable) accession number: Q6GJH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program