ID PRPS1_BOVIN Reviewed; 318 AA. AC Q2HJ58; A5PKB5; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 131. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal medulla, and Uterus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. 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; Evidence={ECO:0000250}; 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; BC113300; AAI13301.1; -; mRNA. DR EMBL; BC142427; AAI42428.1; -; mRNA. DR RefSeq; NP_001039654.1; NM_001046189.2. DR AlphaFoldDB; Q2HJ58; -. DR SMR; Q2HJ58; -. DR STRING; 9913.ENSBTAP00000026261; -. DR PaxDb; 9913-ENSBTAP00000026261; -. DR PeptideAtlas; Q2HJ58; -. DR Ensembl; ENSBTAT00000026261.6; ENSBTAP00000026261.5; ENSBTAG00000019703.6. DR GeneID; 781227; -. DR KEGG; bta:781227; -. DR CTD; 5631; -. DR VEuPathDB; HostDB:ENSBTAG00000019703; -. DR VGNC; VGNC:53800; PRPS1. DR eggNOG; KOG1448; Eukaryota. DR GeneTree; ENSGT00950000182803; -. DR HOGENOM; CLU_033546_4_0_1; -. DR InParanoid; Q2HJ58; -. DR OMA; FGWARQD; -. DR OrthoDB; 276387at2759; -. DR TreeFam; TF106366; -. DR Reactome; R-BTA-73843; 5-Phosphoribose 1-diphosphate biosynthesis. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000009136; Chromosome X. DR Bgee; ENSBTAG00000019703; Expressed in adenohypophysis and 107 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; ISS:UniProtKB. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0046101; P:hypoxanthine biosynthetic process; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; 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:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro. DR GO; GO:0034418; P:urate biosynthetic process; IEA:Ensembl. 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. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..318 FT /note="Ribose-phosphate pyrophosphokinase 1" FT /id="PRO_0000244988" 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" 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 //