KPRS1_SPIOL
ID KPRS1_SPIOL Reviewed; 336 AA.
AC Q9XG98;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 1;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 1;
GN Name=PRS1;
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 -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AJ006940; CAB43599.1; -; mRNA.
DR AlphaFoldDB; Q9XG98; -.
DR SMR; Q9XG98; -.
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; Kinase; Magnesium; Metal-binding; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..336
FT /note="Ribose-phosphate pyrophosphokinase 1"
FT /id="PRO_0000141101"
FT REGION 236..251
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 336 AA; 36606 MW; BD797280922B5347 CRC64;
MDQQSFPSFM ASTHFDSSIN RNDTRLRIFS GTANPALAQE IACYMGLQLG KIKIKRFADG
EIYVQLQESV RGCDVFLVQP TCPPANENLM ELLIMIDACR RASAKNITAV IPYFGYARAD
RKTQGRESIA AKLVANLITE AGANRVLACD LHSGQSMGYF DIPVDHVYGQ PVILDYLASK
TICSDDLVVV SPDVGGVARA RAFAKKLSDA PLAIVDKRRH GHNVAEVMNL IGDVKGKVAV
MVDDMIDTAG TISKGAALLH QEGAREVYAC STHAVFSPPA IERLSSGLFQ EVIITNTIPV
LEKNYFPQLT VLSVANLLGE TIWRVHDDCS VSSIFQ
