KPPR_CHLRE
ID KPPR_CHLRE Reviewed; 375 AA.
AC P19824;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phosphoribulokinase, chloroplastic;
DE Short=PRK;
DE Short=PRKase;
DE EC=2.7.1.19;
DE AltName: Full=Phosphopentokinase;
DE Flags: Precursor;
GN Name=PRKA;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=16667433; DOI=10.1104/pp.93.1.188;
RA Roesler K.R., Ogren W.L.;
RT "Chlamydomonas reinhardtii phosphoribulokinase: sequence, purification and
RT kinetics.";
RL Plant Physiol. 93:188-193(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2137;
RA Smith B.D., Spreitzer R.J.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MUTANT 12-2B.
RX PubMed=16668789; DOI=10.1104/pp.98.4.1285;
RA Roesler K.R., Marcotte B.L., Ogren W.L.;
RT "Functional importance of arginine 64 in Chlamydomonas reinhardtii
RT phosphoribulokinase.";
RL Plant Physiol. 98:1285-1289(1992).
RN [4]
RP SUBUNIT.
RX PubMed=12846565; DOI=10.1021/bi034474x;
RA Graciet E., Gans P., Wedel N., Lebreton S., Camadro J.-M., Gontero B.;
RT "The small protein CP12: a protein linker for supramolecular complex
RT assembly.";
RL Biochemistry 42:8163-8170(2003).
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 -!- SUBUNIT: Component of a complex that contains two dimers of PRK, two
CC tetramers of GAPDH and CP12. {ECO:0000269|PubMed:12846565}.
CC -!- INTERACTION:
CC P19824; A6Q0K5: CP12; NbExp=2; IntAct=EBI-9538490, EBI-9538486;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the phosphoribulokinase family. {ECO:0000305}.
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DR EMBL; M36123; AAA33090.1; -; mRNA.
DR EMBL; AF228914; AAF36402.1; -; Genomic_DNA.
DR PIR; T08167; T08167.
DR RefSeq; XP_001694038.1; XM_001693986.1.
DR PDB; 6H7G; X-ray; 2.60 A; A/B=32-375.
DR PDBsum; 6H7G; -.
DR AlphaFoldDB; P19824; -.
DR SASBDB; P19824; -.
DR SMR; P19824; -.
DR IntAct; P19824; 1.
DR MINT; P19824; -.
DR STRING; 3055.EDP02974; -.
DR PRIDE; P19824; -.
DR ProMEX; P19824; -.
DR EnsemblPlants; PNW75922; PNW75922; CHLRE_12g554800v5.
DR GeneID; 5719722; -.
DR Gramene; PNW75922; PNW75922; CHLRE_12g554800v5.
DR KEGG; cre:CHLRE_12g554800v5; -.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_033590_1_0_1; -.
DR OMA; GLKMRAT; -.
DR OrthoDB; 1022120at2759; -.
DR BRENDA; 2.7.1.19; 1318.
DR UniPathway; UPA00116; -.
DR GO; GO:0009507; C:chloroplast; IDA:CAFA.
DR GO; GO:0010319; C:stromule; IEA:EnsemblPlants.
DR GO; GO:0099080; C:supramolecular complex; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:EnsemblPlants.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0008974; F:phosphoribulokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calvin cycle; Chloroplast;
KW Direct protein sequencing; Disulfide bond; Kinase; Nucleotide-binding;
KW Photosynthesis; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT CHAIN 32..375
FT /note="Phosphoribulokinase, chloroplastic"
FT /id="PRO_0000025752"
FT DISULFID 47..86
FT /evidence="ECO:0000250"
FT VARIANT 95
FT /note="R -> C (in mutant 12-2B; increase in substrate
FT affinity)"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:6H7G"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:6H7G"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6H7G"
FT TURN 200..209
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:6H7G"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:6H7G"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:6H7G"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:6H7G"
FT HELIX 348..368
FT /evidence="ECO:0007829|PDB:6H7G"
SQ SEQUENCE 375 AA; 41892 MW; 49B94DD7FB974FA2 CRC64;
MAFTMRAPAP RATAQSRVTA NRARRSLVVR ADKDKTVVIG LAADSGCGKS TFMRRMTSIF
GGVPKPPAGG NPDSNTLISD MTTVICLDDY HCLDRNGRKV KGVTALAPEA QNFDLMYNQV
KALKEGKSVD KPIYNHVSGL IDAPEKIESP PILVIEGLHP FYDKRVAELL DFKIYLDISD
DIKFAWKIQR DMAERGHSLE SIKSSIAARK PDFDAYIDPQ KKDADMIIQV LPTQLVPDDK
GQYLRVRLIM KEGSKMFDPV YLFDEGSTIS WIPCGRKLTC SFPGIKMFYG PDTWYGQEVS
VLEMDGQFDK LEELIYVESH LSNTSAKFYG EITQQMLKNS GFPGSNNGTG LFQTIVGLKV
REVYERIVKK DVVPV
