Q5R8F8 (PRPS2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribose-phosphate pyrophosphokinase 2
EC=2.7.6.1

Alternative name(s):
Phosphoribosyl pyrophosphate synthase II
Short name=PRS-II

Gene names

Name:

PRPS2

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Ponginae › Pongo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by magnesium and inorganic phosphate.
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.
Subunit structure	Homodimer. The active form is probably a hexamer composed of 3 homodimers By similarity.
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 Reference proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway nucleoside metabolic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB ribose phosphate diphosphokinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 318	317	Ribose-phosphate pyrophosphokinase 2		PRO_0000290002
Regions
	Nucleotide binding	96 – 101	6	ATP By similarity
	Region	212 – 227	16	Binding of phosphoribosylpyrophosphate Potential
Sites
	Metal binding	128	1	Magnesium Potential
	Metal binding	130	1	Magnesium Potential
	Metal binding	139	1	Magnesium Potential
	Metal binding	143	1	Magnesium Potential
	Binding site	130	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R8F8 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 72A2873408250C31	FASTA	318	34,769
	10 20 30 40 50 60 MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC 70 80 90 100 110 120 GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG 130 140 150 160 170 180 ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIA EWKNCIIVSP DAGGAKRVTS 190 200 210 220 230 240 IADRLNVEFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG 250 260 270 280 290 300 ATKVYAILTH GIFSGPAISR INNAAFEAVV VTNTIPQEDK MKHCTKIQVI DISMILAEAI 310 RRTHNGESVS YLFSHVPL

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR859794 mRNA. Translation: CAH91952.1.
RefSeq	NP_001128998.1. NM_001135526.1.
UniGene	Pab.19726.
3D structure databases
HSSP	HSSP built from PDB template 1DKU based on UniProtKB P14193.
ProteinModelPortal	Q5R8F8.
ModBase	Search...
Proteomic databases
PRIDE	Q5R8F8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100190838.
KEGG	pon:100190838.
Organism-specific databases
CTD	5634.
Phylogenomic databases
HOVERGEN	HBG001520.
InParanoid	Q5R8F8.
KO	K00948.
Enzyme and pathway databases
UniPathway	UPA00087; UER00172.
Family and domain databases
InterPro	IPR000842. PRib_PP_synth_CS. IPR000836. PRibTrfase_dom. IPR005946. Rib-P_diPkinase. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. ribP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRPS2_PONAB

Accession

Primary (citable) accession number: Q5R8F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program