ID   KPPR_WHEAT              Reviewed;         404 AA.
AC   P26302;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Phosphoribulokinase, chloroplastic;
DE            Short=PRK;
DE            Short=PRKase;
DE            EC=2.7.1.19;
DE   AltName: Full=Phosphopentokinase;
DE   Flags: Precursor;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2558286;
RA   Raines C.A., Longstaff M., Lloyd J.C., Dyer T.A.;
RT   "Complete coding sequence of wheat phosphoribulokinase: developmental and
RT   light-dependent expression of the mRNA.";
RL   Mol. Gen. Genet. 220:43-48(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring; TISSUE=Etiolated shoot;
RX   PubMed=1651129; DOI=10.1007/bf00036823;
RA   Lloyd J.C., Horsnell P.H., Dyer T.A., Raines C.A.;
RT   "Structure and sequence of a wheat phosphoribulokinase gene.";
RL   Plant Mol. Biol. 17:167-168(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:19365, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57870, ChEBI:CHEBI:58121,
CC         ChEBI:CHEBI:456216; EC=2.7.1.19;
CC   -!- ACTIVITY REGULATION: Light regulated via thioredoxin by reversible
CC       oxidation/reduction of sulfhydryl/disulfide groups.
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the phosphoribulokinase family. {ECO:0000305}.
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DR   EMBL; X51608; CAB56544.1; -; mRNA.
DR   EMBL; X57952; CAA41020.1; -; Genomic_DNA.
DR   PIR; S16585; S16585.
DR   AlphaFoldDB; P26302; -.
DR   SMR; P26302; -.
DR   STRING; 4565.Traes_6DL_22C536081.1; -.
DR   PRIDE; P26302; -.
DR   EnsemblPlants; TraesCS6D02G247400.1; TraesCS6D02G247400.1; TraesCS6D02G247400.
DR   Gramene; TraesCS6D02G247400.1; TraesCS6D02G247400.1; TraesCS6D02G247400.
DR   eggNOG; KOG4203; Eukaryota.
DR   HOGENOM; CLU_033590_1_0_1; -.
DR   OMA; GLKMRAT; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000019116; Unplaced.
DR   Genevisible; P26302; TA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008974; F:phosphoribulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006082; PRK.
DR   InterPro; IPR006083; PRK/URK.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00478; PHRIBLKINASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00567; PHOSPHORIBULOKINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calvin cycle; Chloroplast; Disulfide bond; Kinase;
KW   Nucleotide-binding; Photosynthesis; Plastid; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..53
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           54..404
FT                   /note="Phosphoribulokinase, chloroplastic"
FT                   /id="PRO_0000025755"
FT   DISULFID        69..108
FT                   /evidence="ECO:0000250"
FT   CONFLICT        8
FT                   /note="T -> S (in Ref. 2; CAA41020)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="F -> L (in Ref. 2; CAA41020)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="D -> G (in Ref. 2; CAA41020)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   404 AA;  45141 MW;  06E9F367BE507DB9 CRC64;
     MAFCSPHTTT SLRSPCTTIP NSGFRQNQVI FFTTRSSRRS NTRHGARTFQ VSCAVEQPIV
     IGLAADSGCG KSTFMRRLTS VFGGAAEPPK GGNPDSNTLI SDTTTVICLD DYHSLDRTGR
     KEKGVTALDP KANDFDLMYE QVKAIKEGKA IEKPIYNHVT GLLDPAELIQ PPKIFVIEGL
     HPMYDERVRE LLDFSIYLDI SNEVKFAWKI QRDMAERGHS LESIKASIEA RKPDFDAFID
     PQKQYADAVI EVLPTQLIPD DNEGKVLRVK LIMKEGIKFF NPVYLFDEGS TINWIPCGRK
     LTCSYPGIKF SYGPDTYFGQ EVSVLEMDGQ FDRLDELIYV ESHLSNLSTK FYGEVTQQML
     KHADFPGSNN GTGLFQTIVG LKIRDLYEQI IAERAGVPAE AAKV