P87171 (KPR4_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribose-phosphate pyrophosphokinase 4
EC=2.7.6.1

Alternative name(s):
Phosphoribosyl pyrophosphate synthase 4

Gene names

Name:	prs4
ORF Names:	SPBC3D6.06c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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. UniProtKB P38063
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 P38063
Subcellular location	Cytoplasm By similarity UniProtKB P38063.
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 Reference proteome
Gene Ontology (GO)
Biological process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe nucleoside metabolic process Inferred from electronic annotation. Source: InterPro ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from sequence or structural similarity. 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: InterPro ribose phosphate diphosphokinase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	Ribose-phosphate pyrophosphokinase 4		PRO_0000309464
Sites
	Metal binding	152	1	Magnesium Potential UniProtKB P38063
	Metal binding	154	1	Magnesium Potential UniProtKB P38063
	Metal binding	167	1	Magnesium Potential UniProtKB P38063

Sequences

	Sequence		Length	Mass (Da)
	P87171 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 3D7348E9AA0F9DC7	FASTA	341	37,338
	10 20 30 40 50 60 MKNLVVFGTE SHPKLTESIC EHLCLDIGRV ELSKFSNGET SVRIKQSVRG CDVYIVSPAS 70 80 90 100 110 120 GQVNDHLMEL LIMISACKTA SAKKVTAVLP VFPYSRQPDQ KFSFSGAPLS DLQDAVVPCK 130 140 150 160 170 180 KQTGYHPWIA QSGTLVADLL MCSGADHIIT MDLHDPQFQG FFDIPVDNLF GRPLLKHYIS 190 200 210 220 230 240 LNIPNYHNAV IVSPDAGGAK RATAIADALG LDFALIHKNR RHEYGTSLML VGDVQNKVAI 250 260 270 280 290 300 LIDDLIDTAY TLVRAAEFVK EHGASKIYAL VTHCVLSGDA IERVKLSCID KLIVTNTAPQ 310 320 330 340 TITPSGCFDI IDVAPTFAEA IRRIHNGESI SILYDHNQVW V

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: 972 / ATCC 24843.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAB09126.1.
PIR	T40366.
RefSeq	NP_595518.1. NM_001021427.1.
3D structure databases
HSSP	HSSP built from PDB template 1DKU based on UniProtKB P14193.
ProteinModelPortal	P87171.
ModBase	Search...
Protein-protein interaction databases
STRING	P87171.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC3D6.06c.1; SPBC3D6.06c.1:pep; SPBC3D6.06c.
GeneID	2541014.
GenomeReviews	Gene locus prs4 in contig CU329671_GR.
KEGG	spo:SPBC3D6.06c.
NMPDR	fig|4896.1.peg.1384.
Organism-specific databases
GeneDB_Spombe	SPBC3D6.06c.
Phylogenomic databases
eggNOG	fuNOG07610.
GeneTree	EFGT00050000003657.
HOGENOM	HBG519284.
OMA	CIMISAC.
OrthoDB	EOG4CG3HW.
Gene expression databases
ArrayExpress	P87171.
Family and domain databases
InterPro	IPR000842. PRib_PP_synth_CS. IPR000836. PRibTrfase. IPR005946. Rib-P_diPkinase. [Graphical view]
KO	K00948.
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. RibP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPR4_SCHPO

Accession

Primary (citable) accession number: P87171

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	July 1, 1997
Last modified:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program