Reviewed, UniProtKB/Swiss-Prot O94413 (KPR3_SCHPO)

Names and origin

Protein names

Recommended name:
    Ribose-phosphate pyrophosphokinase 3
    EC=2.7.6.1
Alternative name(s):
    Phosphoribosyl pyrophosphate synthetase 3

Gene names

Name:	prs3
ORF Names:	SPCC1620.06c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	5-phosphoribose 1-diphosphate synthetase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthetases By similarity.
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. UniProtKB P38689
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. UniProtKB P38689
Subcellular location	Cytoplasm. Ref.2
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
PTM	Phosphoprotein
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: InterPro
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
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: UniProtKB-KW ribose phosphate diphosphokinase activity Inferred from electronic annotation. Source: EC
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 3		PRO_0000309463
Sites
	Metal binding	130	1	Magnesium Potential UniProtKB P38689
	Metal binding	132	1	Magnesium Potential UniProtKB P38689
	Metal binding	145	1	Magnesium Potential UniProtKB P38689
Amino acid modifications
	Modified residue	172	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O94413-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 584DFE1EC5C36DD5	FASTA	321	34,779
	10 20 30 40 50 60 MASNSIKIFA GNSHPELAEK VARRIGLSLG KVAVVQYSNR ETSVTIGESV RDEDVFILQT 70 80 90 100 110 120 GCGSINDHLM ELLIMINACR SASARRITAI IPCFPYARQD KKDKSRAPIT ARLVANMLQT 130 140 150 160 170 180 AGCNHIITMD LHASQIQGFF NVPVDNLYAE PSVLRYIREN IDTTVNPTVI VSPDAGGAKR 190 200 210 220 230 240 ATALADRLDL DFALIHKERQ KANEVSRMVL VGDVRDKLAI LVDDMADTCG TLGLAAKTLK 250 260 270 280 290 300 DNGAKAVYAI VTHGILSGKA IKVINESALE KVIVTNTIPH DDKRSLCSKI ETIDISGVLA 310 320 ECIRRIHHGE SVSVLFSVAP A

References

[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA22490.1.
PIR	T41036.
RefSeq	NP_588464.1.
3D structure databases
HSSP	HSSP built from PDB template 1DKR based on UniProtKB P14193.
SMR	O94413. Positions 5-320.
ModBase	Search...
Protein-protein interaction databases
STRING	O94413.
Genome annotation databases
GeneID	2538924.
GenomeReviews	Gene locus prs3 in contig CU329672_GR.
KEGG	spo:SPCC1620.06c.
NMPDR	fig|4896.1.peg.802.
Organism-specific databases
GeneDB_Spombe	SPCC1620.06c.
Phylogenomic databases
OMA	PKIQCID.
Enzyme and pathway databases
BRENDA	2.7.6.1. 653.
Gene expression databases
ArrayExpress	O94413.
Family and domain databases
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

KPR3_SCHPO

Accession

Primary (citable) accession number: O94413

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)