PRPS1_BOVIN
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 03-AUG-2022, entry version 125.
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}.
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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; Q2HJ58; -.
DR PeptideAtlas; Q2HJ58; -.
DR PRIDE; Q2HJ58; -.
DR Ensembl; ENSBTAT00000026261; ENSBTAP00000026261; ENSBTAG00000019703.
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; 1043963at2759; -.
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 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: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 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 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
