P41831 (KPR1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribose-phosphate pyrophosphokinase 1
EC=2.7.6.1

Alternative name(s):
Phosphoribosyl pyrophosphate synthase 1

Gene names

ORF Names:

SPAC4A8.14

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases By similarity.
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.
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.
Subcellular location	Cytoplasm Ref.3.
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 Reference proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide metabolic process Non-traceable author statement. Source: PomBase ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay Ref.3. Source: PomBase nucleus Inferred from direct assay Ref.3. Source: PomBase
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: InterPro ribose phosphate diphosphokinase activity Inferred from sequence orthology. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 409	409	Ribose-phosphate pyrophosphokinase 1		PRO_0000141091
Sites
	Metal binding	128	1	Magnesium Potential
	Metal binding	130	1	Magnesium Potential
	Metal binding	143	1	Magnesium Potential
Amino acid modifications
	Modified residue	199	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P41831 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 08157F6E93F2BFC6	FASTA	409	45,353
	10 20 30 40 50 60 MKSATIIGGG SHPELLHLIS NRLGITPCDV SLKRFANGET SVEIRESVRD KDVFILQSGS 70 80 90 100 110 120 STVNDSLMEL LIIISACKGG SAKRITAVMP YFPYSKQSKM RKYRDAITAR MVANLLTVAG 130 140 150 160 170 180 VDHIITLDLH ASQMQGFFTR PVDNLYAEPN IAEWIRRNVD DWEEAVVVSK NPGGAKRVTS 190 200 210 220 230 240 LADTLNLDFA LINTDRQRSS HFSQNFEDSI MDETEATETH VTNCSVYLDR PRIHTAKYLL 250 260 270 280 290 300 GHIIDDEEII TTPASVCSED YAQEVNLYSQ GGCPSDDDEE ENIMSASIYA ERMITLVGDV 310 320 330 340 350 360 NGKTALLIDD TIENPTAFIV ASEHLVKRCG AKRVIVIGTH GIFQNKCLKD LQSCEYIEQI 370 380 390 400 VVTNTYPIKP QAVLECDKLT VIDISGVLAE AIRRTHNGES ISFLFKKAF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Hilti N. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X83866 Genomic DNA. Translation: CAA58747.1. CU329670 Genomic DNA. Translation: CAB11484.1.
PIR	S51326.
RefSeq	NP_593826.1. NM_001019255.2.
3D structure databases
ProteinModelPortal	P41831.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4690132.
STRING	4896.SPAC4A8.14-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC4A8.14.1; SPAC4A8.14.1:pep; SPAC4A8.14.
GeneID	2543525.
KEGG	spo:SPAC4A8.14.
Organism-specific databases
PomBase	SPAC4A8.14.
Phylogenomic databases
eggNOG	COG0462.
HOGENOM	HOG000210451.
KO	K00948.
OMA	VTNTYPI.
OrthoDB	EOG47WRX7.
Enzyme and pathway databases
UniPathway	UPA00087; UER00172.
Family and domain databases
InterPro	IPR000842. PRib_PP_synth_CS. IPR005946. Rib-P_diPkinase. [Graphical view]
TIGRFAMs	TIGR01251. ribP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20804535.

Entry information

Entry name

KPR1_SCHPO

Accession

Primary (citable) accession number: P41831

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program