KPPR_ARATH
ID KPPR_ARATH Reviewed; 395 AA.
AC P25697;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 OrderedLocusNames=At1g32060; ORFNames=T12O21.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. C24;
RX PubMed=1651130; DOI=10.1007/bf00036828;
RA Horsnell P.R., Raines C.A.;
RT "Nucleotide sequence of a cDNA clone encoding chloroplast
RT phosphoribulokinase from Arabidopsis thaliana.";
RL Plant Mol. Biol. 17:183-184(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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; X58149; CAA41155.1; -; mRNA.
DR EMBL; AC074309; AAG50797.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31430.1; -; Genomic_DNA.
DR EMBL; AY044335; AAK73276.1; -; mRNA.
DR EMBL; AY128355; AAM91558.1; -; mRNA.
DR EMBL; BT000019; AAN15338.1; -; mRNA.
DR EMBL; AY084576; AAM61142.1; -; mRNA.
DR PIR; S16583; S16583.
DR RefSeq; NP_174486.1; NM_102940.6.
DR PDB; 6H7H; X-ray; 2.47 A; A/B=47-395.
DR PDB; 6KEW; X-ray; 2.29 A; A/B=47-395.
DR PDB; 6KEX; X-ray; 2.50 A; A/B/C/D=47-395.
DR PDB; 6KEZ; X-ray; 3.50 A; I/J/K/L=47-395.
DR PDBsum; 6H7H; -.
DR PDBsum; 6KEW; -.
DR PDBsum; 6KEX; -.
DR PDBsum; 6KEZ; -.
DR AlphaFoldDB; P25697; -.
DR SMR; P25697; -.
DR BioGRID; 25332; 7.
DR IntAct; P25697; 2.
DR STRING; 3702.AT1G32060.1; -.
DR iPTMnet; P25697; -.
DR MetOSite; P25697; -.
DR SWISS-2DPAGE; P25697; -.
DR World-2DPAGE; 0003:P25697; -.
DR PaxDb; P25697; -.
DR PRIDE; P25697; -.
DR ProteomicsDB; 250765; -.
DR EnsemblPlants; AT1G32060.1; AT1G32060.1; AT1G32060.
DR GeneID; 840098; -.
DR Gramene; AT1G32060.1; AT1G32060.1; AT1G32060.
DR KEGG; ath:AT1G32060; -.
DR Araport; AT1G32060; -.
DR TAIR; locus:2195366; AT1G32060.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_033590_1_0_1; -.
DR InParanoid; P25697; -.
DR OMA; DPPELIN; -.
DR OrthoDB; 1022120at2759; -.
DR PhylomeDB; P25697; -.
DR BioCyc; ARA:AT1G32060-MON; -.
DR BioCyc; MetaCyc:AT1G32060-MON; -.
DR BRENDA; 2.7.1.19; 399.
DR UniPathway; UPA00116; -.
DR PRO; PR:P25697; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P25697; baseline and differential.
DR Genevisible; P25697; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0099080; C:supramolecular complex; IDA:CAFA.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0008974; F:phosphoribulokinase activity; IDA:CAFA.
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; IEP:TAIR.
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; Disulfide bond;
KW Kinase; Nucleotide-binding; Photosynthesis; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT CHAIN 47..395
FT /note="Phosphoribulokinase, chloroplastic"
FT /id="PRO_0000025751"
FT DISULFID 61..100
FT /evidence="ECO:0000250"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:6KEW"
FT TURN 58..62
FT /evidence="ECO:0007829|PDB:6KEZ"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:6KEW"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:6KEW"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6H7H"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 255..268
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:6KEW"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:6KEW"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:6KEW"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:6KEW"
FT HELIX 363..388
FT /evidence="ECO:0007829|PDB:6KEW"
SQ SEQUENCE 395 AA; 44464 MW; 4660A92EF7E39BC6 CRC64;
MAVSTIYSTQ ALNSTHFLTS SSSSKQVFLY RRQPQTNRRF NTLITCAQET IVIGLAADSG
CGKSTFMRRL TSVFGGAAKP PKGGNPDSNT LISDTTTVIC LDDYHSLDRY GRKEQKVTAL
DPRANDFDLM YEQVKALKNG IAVEKPIYNH VTGLLDPPEL IQPPKILVIE GLHPMFDERV
RDLLDFSIYL DISNEVKFAW KIQRDMAERG HSLESIKASI EARKPDFDAF IDPQKQYADA
VIEVLPTTLI PDDNEGKVLR VRLIMKEGVK YFSPVYLFDE GSTISWIPCG RKLTCSYPGI
KFNYEPDSYF DHEVSVLEMD GQFDRLDELI YVESHLSNLS TKFYGEVTQQ MLKHADFPGS
NNGTGLFQTI VGLKIRDLYE QLIANKATAR AEAKA
