ID   KPPR_VITSX              Reviewed;          89 AA.
AC   P85112;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Phosphoribulokinase, chloroplastic;
DE            Short=PRK;
DE            Short=PRKase;
DE            EC=2.7.1.19;
DE   AltName: Full=Phosphopentokinase;
DE   Flags: Fragments;
OS   Vitis sp. (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis; unclassified Vitis.
OX   NCBI_TaxID=3604;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=V.aestivalis X V.lincecumi cv. Suwannee {ECO:0000269|Ref.1};
RC   TISSUE=Leaf {ECO:0000269|Ref.1};
RA   Katam R., Vasanthaiah H.K.N., Basha S.M., McClung S.;
RT   "Suppression of polypeptides in response to water stress in Florida hybrid
RT   grape.";
RL   Submitted (FEB-2007) to UniProtKB.
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; Evidence={ECO:0000305};
CC   -!- ACTIVITY REGULATION: Light regulated via thioredoxin by reversible
CC       oxidation/reduction of sulfhydryl/disulfide groups. {ECO:0000305}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the phosphoribulokinase family. {ECO:0000255}.
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DR   AlphaFoldDB; P85112; -.
DR   SMR; P85112; -.
DR   UniPathway; UPA00116; -.
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   InterPro; IPR006083; PRK/URK.
DR   Pfam; PF00485; PRK; 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   Transferase.
FT   CHAIN           1..>89
FT                   /note="Phosphoribulokinase, chloroplastic"
FT                   /id="PRO_0000284766"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        ?..31
FT                   /evidence="ECO:0000250|UniProtKB:P09559"
FT   NON_CONS        40..41
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        60..61
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        72..73
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         89
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   89 AA;  9833 MW;  3C0F524F51CB84F5 CRC64;
     LTSVFGGAAE PPRGGNPDSN TLISDTTTVI CLDDYHSLDR GVTALDPRAN DFDLMYEQVK
     KPDFDAYIDP QKLDELIYVE SHLSNLSTK