PRPS2_RAT
ID PRPS2_RAT Reviewed; 318 AA.
AC P09330; Q63462;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 2;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase II;
DE Short=PRS-II;
GN Name=Prps2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2822704; DOI=10.1016/s0021-9258(18)48105-7;
RA Taira M., Ishijima S., Kita K., Yamada K., Iizasa T., Tatibana M.;
RT "Nucleotide and deduced amino acid sequences of two distinct cDNAs for rat
RT phosphoribosylpyrophosphate synthetase.";
RL J. Biol. Chem. 262:14867-14870(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2555778; DOI=10.1093/nar/17.21.8859;
RA Ishijima S., Taira M., Tatibana M.;
RT "Complete cDNA sequence of rat phosphoribosylpyrophosphate synthetase
RT subunit II (PRS II).";
RL Nucleic Acids Res. 17:8859-8859(1989).
RN [3]
RP PROTEIN SEQUENCE OF 185-194, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP)
CC that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Activated by magnesium and inorganic phosphate.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed of 3
CC homodimers (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M17259; AAA41964.1; -; mRNA.
DR EMBL; M29393; AAA41961.1; -; mRNA.
DR EMBL; X16555; CAA34556.1; -; mRNA.
DR PIR; B29463; KIRTR2.
DR RefSeq; NP_036766.1; NM_012634.1.
DR AlphaFoldDB; P09330; -.
DR SMR; P09330; -.
DR BioGRID; 246821; 1.
DR IntAct; P09330; 1.
DR STRING; 10116.ENSRNOP00000005615; -.
DR jPOST; P09330; -.
DR PaxDb; P09330; -.
DR PRIDE; P09330; -.
DR GeneID; 24689; -.
DR KEGG; rno:24689; -.
DR CTD; 5634; -.
DR RGD; 3415; Prps2.
DR VEuPathDB; HostDB:ENSRNOG00000004160; -.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_4_0_1; -.
DR InParanoid; P09330; -.
DR OMA; WSRAPIS; -.
DR OrthoDB; 1043963at2759; -.
DR PhylomeDB; P09330; -.
DR TreeFam; TF106366; -.
DR Reactome; R-RNO-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR SABIO-RK; P09330; -.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P09330; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000004160; Expressed in ovary and 20 other tissues.
DR Genevisible; P09330; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IDA:RGD.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0016208; F:AMP binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0019003; F:GDP binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IDA:RGD.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IDA:RGD.
DR GO; GO:0006167; P:AMP biosynthetic process; IDA:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IDA:RGD.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IDA:RGD.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..318
FT /note="Ribose-phosphate pyrophosphokinase 2"
FT /id="PRO_0000141077"
FT REGION 212..227
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 96..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT CONFLICT 235
FT /note="K -> N (in Ref. 1; AAA41961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 34813 MW; A4674F6BE6667F2F CRC64;
MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC
GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIT EWRNCIIVSP DAGGAKRVTS
IADRLNVEFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG
ATKVYAILTH GIFSGPAISR INNAAFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI
RRTHNGESVS YLFSHVPL
