KPRS3_SPIOL
ID KPRS3_SPIOL Reviewed; 406 AA.
AC Q9XGA0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 3, mitochondrial;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 3;
DE Flags: Precursor;
GN Name=PRS3;
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: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AJ006942; CAB43601.1; -; mRNA.
DR AlphaFoldDB; Q9XGA0; -.
DR SMR; Q9XGA0; -.
DR PRIDE; Q9XGA0; -.
DR OrthoDB; 893352at2759; -.
DR GO; GO:0005739; C:mitochondrion; 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 CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 2.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide biosynthesis; Nucleotide-binding; Transferase; Transit peptide.
FT TRANSIT 1..87
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 88..406
FT /note="Ribose-phosphate pyrophosphokinase 3, mitochondrial"
FT /id="PRO_0000016846"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..324
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 45437 MW; 9374BDD6FC499ABF CRC64;
MAATPHRHLL QPCKNPAISS SETLKPSSSF SLSSNPSIPL IRRRLPTFRC DFQNRRKWMN
VDHHISKLNP IQIVPNSRRF QMSSNQENSV EFSKKVCLFY CPETKALAER IAAQSDAIQL
RSISWRTFED GFPNLFISNA QGIRGKHVAF LASFSSPGVI FEQLSVIYAL PKLFVASFKL
VLPFFPTGTS ERMEDEGDVA TAFTLARILS NIPISREGPT SLVTFDIHAL QERFYFGDNI
LPCFESGIPL LKKKLQQLPD SDNITIAFPD DGAWKRFHKQ LQHFPMIVCA KVREGDQRIV
RLKEGDPTGR HVVIVDDLVQ SGGTLIECQK VLAAHGAAKV SAYVTHGIFP NKSWERFKPD
TAGCPEEGMT HFWITDSCPL TVKMVKNRPP FEVISLAGSI AAALQI
