Reviewed, UniProtKB/Swiss-Prot Q680A5 (KPRS4_ARATH)

Names and origin

Protein names

Recommended name:
    Ribose-phosphate pyrophosphokinase 4
    EC=2.7.6.1
Alternative name(s):
    Phosphoribosyl pyrophosphate synthetase 4

Gene names

Name:	PRS4
Ordered Locus Names:	At2g42910
ORF Names:	F23E6.7, F7D19.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
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 nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR
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 – 337	337	Ribose-phosphate pyrophosphokinase 4		PRO_0000141095
Regions
	Region	241 – 256	16	Binding of phosphoribosylpyrophosphate Potential
Sites
	Metal binding	158	1	Magnesium Potential
	Metal binding	160	1	Magnesium Potential
Experimental info
	Sequence conflict	293	1	K → R in BAD43725. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q680A5-1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: AF17B157D3B70022	FASTA	337	37,560
	10 20 30 40 50 60 MSENAANNIM ETKICTDAIV SELQKKKVHL FYCLECEELA RNIAAESDHI TLQSINWRSF 70 80 90 100 110 120 ADGFPNLFIN NAHDIRGQHV AFLASFSSPA VIFEQISVIY LLPRLFVASF TLVLPFFPTG 130 140 150 160 170 180 SFERMEEEGD VATAFTMARI VSNIPISRGG PTSVVIYDIH ALQERFYFAD QVLPLFETGI 190 200 210 220 230 240 PLLTKRLQQL PETEKVIVAF PDDGAWKRFH KLLDHYPTVV CTKVREGDKR IVRLKEGNPA 250 260 270 280 290 300 GCHVVIVDDL VQSGGTLIEC QKVLAAHGAV KVSAYVTHGV FPKSSWERFT HKKNGLEEAF 310 320 330 AYFWITDSCP QTVKAIGNKA PFEVLSLAGS IADALQI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of cDNAs specifying a novel class of phosphoribosyl diphosphate synthase in Arabidopsis thaliana." Krath B.N., Eriksen T.A., Poulsen T.S., Hove-Jensen B. Biochim. Biophys. Acta 1430:403-408(1999) [PubMed: 10082968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 246-337. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ012407 mRNA. Translation: CAB43553.1. AC006580 Genomic DNA. Translation: AAM15296.1. AC006931 Genomic DNA. Translation: AAD21718.1. AY128402 mRNA. Translation: AAM91605.1. BT000083 mRNA. Translation: AAN15402.1. AY087406 mRNA. Translation: AAM64955.1. AK175962 mRNA. Translation: BAD43725.1.
IPI	IPI00545291.
PIR	T52589.
RefSeq	NP_181819.1.
UniGene	At.425
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q680A5.
Proteomic databases
PRIDE	Q680A5.
Genome annotation databases
GeneID	818892.
GenomeReviews	Gene locus AT2G42910 in contig CT485783_GR.
KEGG	ath:AT2G42910.
NMPDR	fig|3702.1.peg.11442.
Organism-specific databases
GeneFarm	4836. 468.
TAIR	At2g42910.
Phylogenomic databases
OMA	QSINWRS.
Enzyme and pathway databases
BRENDA	2.7.6.1. 302.
Gene expression databases
Genevestigator	Q680A5.
GermOnline	AT2G42910. Arabidopsis thaliana.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPRS4_ARATH

Accession

Primary (citable) accession number: Q680A5
Secondary accession number(s): Q9S7B9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	November 3, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)