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PRPSB_DICDI
ID   PRPSB_DICDI             Reviewed;         329 AA.
AC   Q75JN8; Q559L5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase B;
DE            EC=2.7.6.1;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase B;
GN   Name=prsB; ORFNames=DDB_G0272246;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000008; EAL71275.1; -; Genomic_DNA.
DR   RefSeq; XP_645319.1; XM_640227.1.
DR   AlphaFoldDB; Q75JN8; -.
DR   SMR; Q75JN8; -.
DR   STRING; 44689.DDB0237883; -.
DR   PaxDb; Q75JN8; -.
DR   EnsemblProtists; EAL71275; EAL71275; DDB_G0272246.
DR   GeneID; 8618485; -.
DR   KEGG; ddi:DDB_G0272246; -.
DR   dictyBase; DDB_G0272246; prsB.
DR   eggNOG; KOG1448; Eukaryota.
DR   HOGENOM; CLU_033546_4_0_1; -.
DR   InParanoid; Q75JN8; -.
DR   OMA; HYAYARS; -.
DR   PhylomeDB; Q75JN8; -.
DR   Reactome; R-DDI-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR   UniPathway; UPA00087; UER00172.
DR   PRO; PR:Q75JN8; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   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; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; SSF53271; 2.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..329
FT                   /note="Ribose-phosphate pyrophosphokinase B"
FT                   /id="PRO_0000328321"
FT   REGION          227..242
FT                   /note="Binding of phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255"
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         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   329 AA;  36145 MW;  17CED30D45044569 CRC64;
     MSNNRLVILH GNAHPKLSKE IASCLNTEVG NALVSKFANS ETQVIINESV RDVDLYIVQP
     TCNPSVNDYL MELLVMVDGA KRASAHRITA VVPFFGYARQ SKKDKSRAPI TCKLVANMME
     AAGIDRVITM DLHSSQIQGF FNIPVENVYT EPLFVKYIKK KKKTEFLNQE FVIVSPGVGG
     VKRAKAISDK LESELAIIHR ANKEMSLSLS SSFSFDIEET VLVGDVTGKI AIIIDDIADT
     CKTLKLASKA LIKKGAIKVY ALVTHGVFSN NAIDIINDSS ITELVITDSI PNEHNKEKCP
     KLKIISIASV LSETMRRCHH GESVTSISK
 
 
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