Q92EF1 (KPRS2_LISIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	lin0509

Organism

Listeria innocua serovar 6a (strain CLIP 11262) [Complete proteome] [HAMAP]

Taxonomic identifier

272626 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria innocua

Protein attributes

Sequence length	311 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_B
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_B
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 – 311	311	Ribose-phosphate pyrophosphokinase 2 HAMAP-Rule MF_00583_B		PRO_0000141153
Regions
	Region	212 – 225	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)
	Q92EF1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 2D12EC4A6264766D	FASTA	311	34,431
	10 20 30 40 50 60 MTGKMKLFSV TSERPLATKI ADYLDIPLCE VELQKFSDGE VKINIEESIR GTNAYVVQSM 70 80 90 100 110 120 NANVNERLME LLIMVDALKR ASVHSINIIM PYYGYARQDR KARSREPITA KLMANLIQRA 130 140 150 160 170 180 GANRLITVDL HAAQIQGFFN IPIDHLSAVP LIGDYLIEKY GEEDVVVVAP DHSGVVRARR 190 200 210 220 230 240 IADRLNAPIA ILNRKPRPHE DEIMSVIGDV KGKVAIVVDD IIDTGVRATT SADILLEKGA 250 260 270 280 290 300 VEVIACATHS VMAGDATERL QNSRIKEVIT SDSIDLPEEK QFEKLTTISI GRILGRAIEG 310 VQENRSLHPL F

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL596165 Genomic DNA. Translation: CAC95741.1.
PIR	AE1496.
RefSeq	NP_469852.1. NC_003212.1.
3D structure databases
ProteinModelPortal	Q92EF1.
SMR	Q92EF1. Positions 4-311.
ModBase	Search...
Protein-protein interaction databases
STRING	272626.lin0509.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC95741; CAC95741; CAC95741.
GeneID	1128961.
KEGG	lin:lin0509.
PATRIC	20297713. VBILisInn102668_0530.
Organism-specific databases
GenoList	LIN0509.
CMR	Search...
Phylogenomic databases
eggNOG	COG0462.
HOGENOM	HOG000210449.
KO	K00948.
OMA	QSMNANV.
ProtClustDB	CLSK563942.
Enzyme and pathway databases
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

KPRS2_LISIN

Accession

Primary (citable) accession number: Q92EF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program