ID   KPR1_CANAX              Reviewed;         321 AA.
AC   P46585;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, 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   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=4918;
RX   PubMed=8553701; DOI=10.1002/yea.320111310;
RA   Payne T.L., Calderone R.A.;
RT   "Isolation of phosphoribosylpyrophosphate synthetase (PRS1) gene from
RT   Candida albicans.";
RL   Yeast 11:1295-1302(1995).
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; U23934; AAA97558.1; -; Genomic_DNA.
DR   PIR; S60393; S60393.
DR   AlphaFoldDB; P46585; -.
DR   SMR; P46585; -.
DR   VEuPathDB; FungiDB:C2_02510W_A; -.
DR   VEuPathDB; FungiDB:CAWG_04019; -.
DR   GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:EnsemblFungi.
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:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
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   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   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   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide biosynthesis;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..321
FT                   /note="Ribose-phosphate pyrophosphokinase 1"
FT                   /id="PRO_0000141085"
FT   BINDING         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  35278 MW;  AC70534163AA5BEB CRC64;
     MSTNSIKLLA SDVHRGLAEL VSKRLGLRLT PSELKRESTG EVQFSIGESV RDEDIFIICQ
     IGSGEVNDRV FELMIMINAC KTASARRITV ILPNFPYARQ DRKDKSRAPI TAKLMADMLT
     TAGCDHVITM DLHASQIQGF FDVPVDNLYA EPSVVRYIKE TIDYSEAIII SSDAGGAKRA
     AGLADRLDLN FELIHKERAR ANEVSRMVLV VDVTDKICVI VDDMADTCGT LAKAAEVLLD
     NNAKDVIAIV THGILSGNAI KNINNSKLKK VVCTNTVPFE DKLKLCLKLD TIDISAVIAE
     SIRRLHNGES ISYLFKNAPC K