ID   PRPS1_RAT               Reviewed;         318 AA.
AC   P60892; P09329; Q5M8A4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase 1;
DE            EC=2.7.6.1;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase I;
DE            Short=PRS-I;
GN   Name=Prps1;
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=2555779; DOI=10.1093/nar/17.21.8860;
RA   Ishijima S., Taira M., Tatibana M.;
RT   "Complete cDNA sequence of rat phosphoribosylpyrophosphate synthetase
RT   subunit I (PRS I).";
RL   Nucleic Acids Res. 17:8860-8860(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2154494; DOI=10.1016/s0021-9258(19)39687-5;
RA   Shimada H., Taira M., Yamada K., Iizasa T., Tatibana M.;
RT   "Structure of the rat PRPS1 gene encoding phosphoribosylpyrophosphate
RT   synthetase subunit I.";
RL   J. Biol. Chem. 265:3956-3960(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 85-96, 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}.
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DR   EMBL; M17258; AAA41963.1; -; mRNA.
DR   EMBL; M29392; AAA41960.1; -; mRNA.
DR   EMBL; X16554; CAA34555.1; -; mRNA.
DR   EMBL; M31084; AAA41959.1; -; Genomic_DNA.
DR   EMBL; M31078; AAA41959.1; JOINED; Genomic_DNA.
DR   EMBL; M31079; AAA41959.1; JOINED; Genomic_DNA.
DR   EMBL; M31080; AAA41959.1; JOINED; Genomic_DNA.
DR   EMBL; M31082; AAA41959.1; JOINED; Genomic_DNA.
DR   EMBL; M31083; AAA41959.1; JOINED; Genomic_DNA.
DR   EMBL; BC078853; AAH78853.1; -; mRNA.
DR   EMBL; BC088149; AAH88149.1; -; mRNA.
DR   PIR; A35465; KIRTR1.
DR   RefSeq; NP_001009694.1; NM_001009694.1.
DR   RefSeq; NP_058939.1; NM_017243.2.
DR   RefSeq; XP_008762879.1; XM_008764657.2.
DR   AlphaFoldDB; P60892; -.
DR   SMR; P60892; -.
DR   BioGRID; 248196; 4.
DR   IntAct; P60892; 5.
DR   STRING; 10116.ENSRNOP00000071101; -.
DR   iPTMnet; P60892; -.
DR   PhosphoSitePlus; P60892; -.
DR   jPOST; P60892; -.
DR   PaxDb; 10116-ENSRNOP00000029405; -.
DR   GeneID; 29562; -.
DR   GeneID; 314140; -.
DR   KEGG; rno:29562; -.
DR   KEGG; rno:314140; -.
DR   UCSC; RGD:61955; rat.
DR   AGR; RGD:1359636; -.
DR   AGR; RGD:61955; -.
DR   CTD; 328099; -.
DR   CTD; 5631; -.
DR   RGD; 61955; Prps1.
DR   VEuPathDB; HostDB:ENSRNOG00000060262; -.
DR   eggNOG; KOG1448; Eukaryota.
DR   HOGENOM; CLU_033546_4_0_1; -.
DR   InParanoid; P60892; -.
DR   OrthoDB; 276387at2759; -.
DR   PhylomeDB; P60892; -.
DR   TreeFam; TF106366; -.
DR   Reactome; R-RNO-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR   SABIO-RK; P60892; -.
DR   UniPathway; UPA00087; UER00172.
DR   PRO; PR:P60892; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000060262; Expressed in cerebellum and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
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:0046101; P:hypoxanthine biosynthetic process; ISO:RGD.
DR   GO; GO:0007399; P:nervous system development; ISO:RGD.
DR   GO; GO:0006098; P:pentose-phosphate shunt; ISO:RGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; ISO:RGD.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; ISO:RGD.
DR   GO; GO:0034418; P:urate biosynthetic process; ISO: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   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210:SF32; RIBOSE-PHOSPHATE DIPHOSPHOKINASE; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
DR   World-2DPAGE; 0004:P60892; -.
DR   Genevisible; P60892; RN.
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 1"
FT                   /id="PRO_0000141073"
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        163
FT                   /note="R -> K (in Ref. 4; AAH88149)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  34834 MW;  46D017E969908BA0 CRC64;
     MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIGESVRG EDVYIVQSGC
     GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG
     ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLKWIRENIS EWRNCTIVSP DAGGAKRVTS
     IADRLNVDFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG
     ATRVYAILTH GIFSGPAISR INNACFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI
     RRTHNGESVS YLFSHVPL
//