ID   B9SPJ7_RICCO            Unreviewed;       407 AA.
AC   B9SPJ7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Ribose-phosphate pyrophosphokinase, putative {ECO:0000313|EMBL:EEF34473.1};
DE            EC=2.7.6.1 {ECO:0000313|EMBL:EEF34473.1};
GN   ORFNames=RCOM_0024540 {ECO:0000313|EMBL:EEF34473.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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         Evidence={ECO:0000256|ARBA:ARBA00000179};
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000256|ARBA:ARBA00006478, ECO:0000256|RuleBase:RU004324}.
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DR   EMBL; EQ974068; EEF34473.1; -; Genomic_DNA.
DR   RefSeq; XP_002527916.1; XM_002527870.2.
DR   AlphaFoldDB; B9SPJ7; -.
DR   STRING; 3988.B9SPJ7; -.
DR   GeneID; 8273494; -.
DR   KEGG; rcu:8273494; -.
DR   eggNOG; KOG1448; Eukaryota.
DR   InParanoid; B9SPJ7; -.
DR   OrthoDB; 5485830at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
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; IBA:GO_Central.
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   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10210:SF45; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 3, CHLOROPLASTIC; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 2.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:EEF34473.1};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727,
KW   ECO:0000256|RuleBase:RU004324};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Transferase {ECO:0000313|EMBL:EEF34473.1}.
FT   DOMAIN          98..212
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
FT   DOMAIN          303..347
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   407 AA;  44908 MW;  A8F82E4D84474820 CRC64;
     MTATSPLRNP LNTITTTTKA SSAAKSPKLS CFLQVNRPSK SKILTVKCDN NHPQNLSLKF
     LSGTDHIIQS SSLSLSKSVS MAAASAQESA SKTMKRVCLF YCDETKALAE RVAAESDAIE
     LRAITWRKFE DGFPNLFIPN AQAIRGQHVA FLASFSSPQV IFEQLSIIYA LPKLFISSFT
     LVLPFFPTGT SERMEDEGDV ATAFTLARIL SNIPTSRGGP TSLVIFDIHA LQERFYFGDN
     ILPFFESGIP LLKNRLQQLP DSDNIAIAFP DDGAWKRFHN QLQHFPMIVC AKVREGNQRI
     VRIKEGDPQG RHVVIVDDLV QSGGTLIECQ KVLADHGAAR ISAYVTHGIF PNRSWERFEF
     DNGGHPGNGL TYFWITDSCP STVREVMNKP PFEVLSLASS IAAALQI
//