ID   PRPS2_XENLA             Reviewed;         318 AA.
AC   Q7ZXC9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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       Competitively or non-competitively inhibited by ADP, 2,3-
CC       bisphosphoglyceride or GDP (By similarity). {ECO:0000250}.
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; BC045049; AAH45049.1; -; mRNA.
DR   RefSeq; NP_001080655.1; NM_001087186.1.
DR   AlphaFoldDB; Q7ZXC9; -.
DR   SMR; Q7ZXC9; -.
DR   MaxQB; Q7ZXC9; -.
DR   DNASU; 380347; -.
DR   GeneID; 380347; -.
DR   KEGG; xla:380347; -.
DR   CTD; 380347; -.
DR   Xenbase; XB-GENE-983991; prps2.L.
DR   OMA; SESCARI; -.
DR   OrthoDB; 1043963at2759; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 380347; Expressed in blastula and 19 other tissues.
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; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..318
FT                   /note="Ribose-phosphate pyrophosphokinase 2"
FT                   /id="PRO_0000294083"
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;  34702 MW;  D9D864A3F17328BE CRC64;
     MPNIVLFSGS SHQDLSQKVA ERLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC
     GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG
     ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIP EWKNSSIVSP DAGGAKRVTS
     IADRLNVEFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTVC HAADKLLSAG
     ATKVYAILTH GIFSGPAISR INNAAFEAVV VTNTIPQDEK MKQCSKIQVI DISMILAEAI
     RRTHNGESVS YLFSHVPL