Reviewed, UniProtKB/Swiss-Prot Q7WNY4 (KPRS_BORBR)

Names and origin

Protein names

Recommended 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:	BB0901

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	310 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 MF_00583
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00583
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 HAMAP MF_00583.
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	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro 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 – 310	310	Ribose-phosphate pyrophosphokinase HAMAP MF_00583		PRO_0000141112
Regions
	Region	208 – 221	14	Binding of phosphoribosylpyrophosphate Potential
Sites
	Metal binding	125	1	Magnesium Potential
	Metal binding	127	1	Magnesium Potential
	Metal binding	136	1	Magnesium Potential
	Metal binding	140	1	Magnesium Potential

Sequences

	Sequence		Length	Mass (Da)
	Q7WNY4-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: EBB858434BDC7802	FASTA	310	33,481
	10 20 30 40 50 60 MIFTGTANTR LAVDVVNHLD MSLGKMTVGR FSDGEVMVEI NENVRGKDVF VLQPTCAPTN 70 80 90 100 110 120 DNLMEIMVMV DALRRASAGR ITAAIPYFGY ARQDRRPRSA RVAISAKVVA NMLQVAGVDR 130 140 150 160 170 180 VLTMDLHADQ IQGFFDIPVD NIYAGPILLG DIWRRNFSNL VVVSPDIGGV VRARALAKQL 190 200 210 220 230 240 EADLAIIDKR RPRANVSEVM NIIGEVDGRT CIIMDDMVDT AGTLCKAAQA LKDRGAGAVY 250 260 270 280 290 300 AYCTHPVLSG GAIERIETSS LDELVVTDTI PLSEQGQACG KIRQLSCAAL LGETILRISN 310 AESVSSLFAD

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640439 Genomic DNA. Translation: CAE31400.1.
RefSeq	NP_887450.1.
3D structure databases
SMR	Q7WNY4. Positions 1-304.
ModBase	Search...
Genome annotation databases
GeneID	2662705.
KEGG	bbr:BB0901.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG519284.
OMA	YKTAGAD.
PhylomeDB	Q7WNY4.
Enzyme and pathway databases
BioCyc	BBRO257310:BB0901-MONOMER.
BRENDA	2.7.6.1. 413.
Family and domain databases
HAMAP	MF_00583_B. RibP_PPkinase_B. [Tree]
InterPro	IPR000842. PRib-PP_synthetase_CS. IPR000836. PRibTrfase. IPR005946. PRPP_kinase. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. ribP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHETASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPRS_BORBR

Accession

Primary (citable) accession number: Q7WNY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)