P59512 (KPRS_BUCBP) 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
Synonyms:	prsA
Ordered Locus Names:	bbp_159

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Baizongia pistaciae)

Protein attributes

Sequence length	315 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 – 315	315	Ribose-phosphate pyrophosphokinase HAMAP-Rule MF_00583		PRO_0000141120
Regions
	Region	213 – 226	14	Binding of phosphoribosylpyrophosphate Potential
Sites
	Metal binding	129	1	Magnesium Potential
	Metal binding	131	1	Magnesium Potential
	Metal binding	140	1	Magnesium Potential
	Metal binding	144	1	Magnesium Potential

Sequences

	Sequence		Length	Mass (Da)
	P59512 [UniParc]. Last modified April 11, 2003. Version 1. Checksum: FE45604F26665043	FASTA	315	34,795
	10 20 30 40 50 60 MSDMKLFSGN SVPKLAESIA NKLYVNLGNA SVGKFSDGEI NVQINENVRG SDVFIIQSTC 70 80 90 100 110 120 FPTNDNLMEL VVMVDALRRA SAGRITAVIP YFGYARQDRR VRSSRVPITA KVVADFFSSV 130 140 150 160 170 180 GIDRVLTVDL HAEQIQGFFD VPVDNVFGSL ILFEDMLKID LKNPIVVSPD IGGVIRARAI 190 200 210 220 230 240 AKLLHDTDMA IIDKRRPHIN FSQVMHVIGE VFNRDCILVD DMIDTGGTLC QAAEALKKRG 250 260 270 280 290 300 ARRVFAYATH PIFSGNAVKN LQNSNIDEVV VCDTIPLSKI IQELPNVRTL TLSSMLAEAI 310 RRISNEESIS AMFEH

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO26893.1.
RefSeq	NP_777788.1. NC_004545.1.
3D structure databases
ProteinModelPortal	P59512.
SMR	P59512. Positions 2-312.
ModBase	Search...
Protein-protein interaction databases
STRING	224915.bbp159.
Proteomic databases
PRIDE	P59512.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO26893; AAO26893; bbp_159.
GeneID	1058575.
KEGG	bab:bbp159.
PATRIC	21245097. VBIBucAph80364_0155.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0462.
KO	K00948.
OMA	TRISPTE.
ProtClustDB	PRK01259.
Enzyme and pathway databases
BioCyc	BAPH224915:GJ9D-159-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_BUCBP

Accession

Primary (citable) accession number: P59512

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	April 11, 2003
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program