ID   KPRS2_SPIOL             Reviewed;         395 AA.
AC   Q9XG99;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase 2, chloroplastic;
DE            EC=2.7.6.1;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase 2;
DE   Flags: Precursor;
GN   Name=PRS2;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=9952445; DOI=10.1104/pp.119.2.497;
RA   Krath B.N., Hove-Jensen B.;
RT   "Organellar and cytosolic localization of four phosphoribosyl diphosphate
RT   synthase isozymes in spinach.";
RL   Plant Physiol. 119:497-506(1999).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ006941; CAB43600.1; -; mRNA.
DR   AlphaFoldDB; Q9XG99; -.
DR   SMR; Q9XG99; -.
DR   OrthoDB; 1043963at2759; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-EC.
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; Chloroplast; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Plastid; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..42
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..395
FT                   /note="Ribose-phosphate pyrophosphokinase 2, chloroplastic"
FT                   /id="PRO_0000016845"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..310
FT                   /note="Binding of phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   395 AA;  42715 MW;  98F83217249F2175 CRC64;
     MASPAPRSLS SSSSSSSSSF CPSISPPPRS PSRASLPFSV KCNTVEPLKL VNGKPSVPIL
     DEQSLPKFLH SKRLESSVNR SNTRLKLFSG LANPALAKEV AWYMGLELGK VKIKRFADGE
     IYVQLEESVR GCDVFIIQPT SPPANENLME LLIMIDACRR ASAKNITAVI PYFGYARADR
     KTQGRESIAA KLVANLITEA GANRVLACDL HSGQSMGYFD IPVDHVYCQP VILDYLASKG
     IASSDLVVVS PDVGGVARAR AFAKKLSDAP LAIVDKRRHA HNVAEVMNLI GDVKGKVAVM
     LDDMIDTAGT ITKGAELLHE EGAREVYACC THAVFSPPAI ERLSSGCFQE VIITNTLPVA
     EKNFFRQLTV LSTANLLGET IWRVHDDSSV SSIFQ