PRPSA_DICDI
ID PRPSA_DICDI Reviewed; 317 AA.
AC Q54PA9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ribose-phosphate pyrophosphokinase A;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase A;
GN Name=prsA; ORFNames=DDB_G0284669;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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 -!- 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 -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000070; EAL65104.1; -; Genomic_DNA.
DR RefSeq; XP_638466.1; XM_633374.1.
DR AlphaFoldDB; Q54PA9; -.
DR SMR; Q54PA9; -.
DR STRING; 44689.DDB0237882; -.
DR PaxDb; Q54PA9; -.
DR EnsemblProtists; EAL65104; EAL65104; DDB_G0284669.
DR GeneID; 8624717; -.
DR KEGG; ddi:DDB_G0284669; -.
DR dictyBase; DDB_G0284669; prsA.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_4_0_1; -.
DR InParanoid; Q54PA9; -.
DR OMA; FGWARQD; -.
DR PhylomeDB; Q54PA9; -.
DR Reactome; R-DDI-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:Q54PA9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
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; ISS:dictyBase.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; ISS:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="Ribose-phosphate pyrophosphokinase A"
FT /id="PRO_0000328320"
FT REGION 212..227
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 317 AA; 34465 MW; 8EDACDFBAA680137 CRC64;
MGDRIKILTG NAHRELASEI SDDLNLALGK AHVGKFSNGE TSVMISESIR DMDVYIIQPT
CNPNVNDNLM ELLIMADAIR RASAHRITAV IPCFGYARQD KKDKSRAPIT GKLVANLIET
AGIDRVITMD LHASQIQGFF NIPVDNLYAE PQIIKYIRKY IPGEKVIVSP DAGGVKRAKS
ISDKLDADLA IIHKERKKAN EVSGMILVGD VKDKVALIVD DMADTCGTLV SACEMLISKG
ATKVYALVTH GVLSGDAIQK LNESSLTELV ITNTIPHAEK AAKCPKIKTI NIAHTLSEAI
RRTHHGESIS SLFSDTK
