ID   KPPR_SPIOL              Reviewed;         402 AA.
AC   P09559;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 98.
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   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2841650; DOI=10.1093/nar/16.14.7192;
RA   Roesler K.R., Ogren W.L.;
RT   "Nucleotide sequence of spinach cDNA encoding phosphoribulokinase.";
RL   Nucleic Acids Res. 16:7192-7192(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-402.
RX   PubMed=2843430; DOI=10.1016/0378-1119(88)90224-7;
RA   Milanez S., Mural R.J.;
RT   "Cloning and sequencing of cDNA encoding the mature form of
RT   phosphoribulokinase from spinach.";
RL   Gene 66:55-63(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 52-69.
RX   PubMed=3004354; DOI=10.1016/0003-9861(86)90185-2;
RA   Porter M.A., Milanez S., Stringer C.D., Hartman F.C.;
RT   "Purification and characterization of ribulose-5-phosphate kinase from
RT   spinach.";
RL   Arch. Biochem. Biophys. 245:14-23(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 52-69.
RA   Porter M.A., Hartman F.C.;
RT   "Commonality of catalytic and regulatory sites of spinach
RT   phosphoribulokinase: characterization of a tryptic peptide that contains an
RT   essential cysteinyl residue.";
RL   Biochemistry 25:7314-7318(1986).
RN   [5]
RP   DISULFIDE BOND, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2826432; DOI=10.1016/s0021-9258(19)57366-5;
RA   Porter M.A., Stringer C.D., Hartman F.C.;
RT   "Characterization of the regulatory thioredoxin site of
RT   phosphoribulokinase.";
RL   J. Biol. Chem. 263:123-129(1988).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA34036.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X07654; CAA30499.1; -; mRNA.
DR   EMBL; M21338; AAA34036.1; ALT_INIT; mRNA.
DR   PIR; S02099; S02099.
DR   AlphaFoldDB; P09559; -.
DR   SMR; P09559; -.
DR   OrthoDB; 276087at2759; -.
DR   BRENDA; 2.7.1.19; 5812.
DR   SABIO-RK; P09559; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP001155700; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   CDD; cd02026; PRK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006082; PRK.
DR   InterPro; IPR006083; PRK/URK.
DR   PANTHER; PTHR10285:SF211; PHOSPHORIBULOKINASE; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00478; PHRIBLKINASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00567; PHOSPHORIBULOKINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calvin cycle; Chloroplast; Direct protein sequencing;
KW   Disulfide bond; Kinase; Nucleotide-binding; Photosynthesis; Plastid;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:3004354, ECO:0000269|Ref.4"
FT   CHAIN           52..402
FT                   /note="Phosphoribulokinase, chloroplastic"
FT                   /id="PRO_0000025754"
FT   DISULFID        67..106
FT                   /evidence="ECO:0000269|PubMed:2826432"
SQ   SEQUENCE   402 AA;  45007 MW;  450759B96A675C6B CRC64;
     MAVCTVYTIP TTTHLGSSFN QNNKQVFFNY KRSSSSNNTL FTTRPSYVIT CSQQQTIVIG
     LAADSGCGKS TFMRRLTSVF GGAAEPPKGG NPDSNTLISD TTTVICLDDF HSLDRNGRKV
     EKVTALDPKA NDFDLMYEQV KALKEGKAVD KPIYNHVSGL LDPPELIQPP KILVIEGLHP
     MYDARVRELL DFSIYLDISN EVKFAWKIQR DMKERGHSLE SIKASIESRK PDFDAYIDPQ
     KQHADVVIEV LPTELIPDDD EGKVLRVRMI QKEGVKFFNP VYLFDEGSTI SWIPCGRKLT
     CSYPGIKFSY GPDTFYGNEV TVVEMDGMFD RLDELIYVES HLSNLSTKFY GEVTQQMLKH
     QNFPGSNNGT GFFQTIIGLK IRDLFEQLVA SRSTATATAA KA
//