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Protein

Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic

Gene

RP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional serine/threonine kinase and phosphorylase involved in the dark/light-mediated regulation of PPDK by catalyzing its phosphorylation/dephosphorylation. Dark/light-induced changes in stromal concentrations of the competing ADP and Pi substrates govern the direction of the reaction. In the dark, phosphorylates the catalytic intermediate of PPDK (PPDK-HisP), inactivating it. Light exposure induces the phosphorolysis reaction that reactivates PPDK. Unlike the kinase function which can utilize either Thr or Ser as target, the phosphorylase function has a strict substrate requirement for threonyl phosphate.2 Publications

Catalytic activityi

ADP + [pyruvate, phosphate dikinase] = AMP + [pyruvate, phosphate dikinase] phosphate.1 Publication
[Pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate.1 Publication

Enzyme regulationi

Regulated by light/dark exposure.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi269 – 2768ADPSequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.32. 399.
2.7.4.27. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic (EC:2.7.11.321 Publication, EC:2.7.4.271 Publication)
Alternative name(s):
Bifunctional dikinase regulatory protein 1
Short name:
AtRP1
Short name:
BFRP1
Pyruvate, Pi dikinase regulatory protein 1
Short name:
PPDK RP1
Short name:
PPDK regulatory protein 1
Gene namesi
Name:RP1
Ordered Locus Names:At4g21210
ORF Names:F7J7.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G21210.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221S → A: No effect on phosphotransferase and kinase activities. 1 Publication
Mutagenesisi123 – 1231D → A: No effect on phosphotransferase and kinase activities. 1 Publication
Mutagenesisi238 – 2381Y → F: No effect on phosphotransferase and kinase activities. 1 Publication
Mutagenesisi252 – 2521D → N: No effect on the interaction with PPDK, but loss of phosphotransferase activity and partially reduced kinase activity. 1 Publication
Mutagenesisi269 – 2691G → A: No effect on the interaction with PPDK, but loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi271 – 2711S → A: No effect on the interaction with PPDK, but loss of phosphotransferase activity and partially reduced kinase activity. 1 Publication
Mutagenesisi272 – 2721R → M: Weak interaction with PPDK, and loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi275 – 2751K → M: Weak interaction with PPDK, and loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi277 – 2771P → A: Weak interaction with PPDK, and loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi279 – 2791S → A: No effect on phosphotransferase and kinase activities. 1 Publication
Mutagenesisi283 – 2831A → T: No effect on the interaction with PPDK, but loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi291 – 2911N → A: No effect on the interaction with PPDK, but loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi293 – 2931P → A: No effect on the interaction with PPDK, but reduced phosphotransferase and kinase activities. 1 Publication
Mutagenesisi326 – 3261R → M: Weak interaction with PPDK, and loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi329 – 3291R → M: No effect on the interaction with PPDK, but loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi343 – 3431Y → F: Weak effect on the interaction with PPDK, but loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi352 – 3521E → Q: Weak interaction with PPDK, and loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi377 – 3771E → Q: Weak interaction with PPDK, and loss of phosphotransferase and kinase activities. 1 Publication
Mutagenesisi378 – 3781E → Q: No effect on phosphotransferase and kinase activities. 1 Publication
Mutagenesisi379 – 3791T → V: No effect on phosphotransferase and kinase activities. 1 Publication
Mutagenesisi380 – 3801A → T: No effect on the interaction with PPDK, but loss of phosphotransferase and kinase activities. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8686ChloroplastSequence analysisAdd
BLAST
Chaini87 – 403317Pyruvate, phosphate dikinase regulatory protein 1, chloroplasticPRO_0000196751Add
BLAST

Proteomic databases

PaxDbiO49562.
PRIDEiO49562.

Expressioni

Tissue specificityi

Expressed in green tissues.1 Publication

Gene expression databases

ExpressionAtlasiO49562. baseline and differential.
GenevisibleiO49562. AT.

Interactioni

Subunit structurei

Interacts with PPDK1.1 Publication

Protein-protein interaction databases

STRINGi3702.AT4G21210.1.

Structurei

3D structure databases

ProteinModelPortaliO49562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 1044Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IFEV. Eukaryota.
COG1806. LUCA.
HOGENOMiHOG000218052.
InParanoidiO49562.
KOiK20115.
OMAiNRAMPRI.
PhylomeDBiO49562.

Family and domain databases

HAMAPiMF_00921. PDRP.
InterProiIPR005177. Kinase-pyrophosphorylase.
IPR026565. PPDK_reg.
IPR017409. Pyrv_Pi_dikinase_reg_chlpt.
[Graphical view]
PfamiPF03618. Kinase-PPPase. 1 hit.
[Graphical view]
PIRSFiPIRSF038149. Pyruvate_Pi_dikinase_regulator. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O49562-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALLSAMKLQ GRPPPISSNL NPNSKPAGSD SVSLNASEPG SERKPRKFSS
60 70 80 90 100
QLNRWNRART LRSGAKLDST ITNGSNNTTG PMRPIESSSR TDVSTLDSDV
110 120 130 140 150
SSSSNGVSEA DMTAAKSIYI VSDGTGWTAE HAVNAALGQF DYCLVDRGCP
160 170 180 190 200
VNTHLFSGIE DGEKLMEIIK QAAREGAMVI YTLADPSMAE ATMRACKLWK
210 220 230 240 250
IPSLDILGPI TESISSHLGT NPSGLSRGIT NSSLNEDYFK RIEAIEFTIK
260 270 280 290 300
HDDGALPENL EKADIVLVGV SRTGKTPLST YLAQKGYKVS NVPIVNGVDL
310 320 330 340 350
PKTLFEIDPR KVFGLMINPL VLQGIREARA KSLGLGSSFK TKYSELGSVK
360 370 380 390 400
EELELAKKIF AENPTWPVIE VTESAIEETA AVVLRLYDER QSNRAMPRIS

KSY
Length:403
Mass (Da):43,684
Last modified:June 1, 1998 - v1
Checksum:i125AF179D5EA6564
GO
Isoform 2 (identifier: O49562-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     297-323: Missing.

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:376
Mass (Da):40,648
Checksum:iAF7E2DAD6395B3FB
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei297 – 32327Missing in isoform 2. CuratedVSP_034504Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021960 Genomic DNA. Translation: CAA17540.1.
AL161554 Genomic DNA. Translation: CAB79121.1.
CP002687 Genomic DNA. Translation: AEE84423.1.
CP002687 Genomic DNA. Translation: AEE84424.1.
AK316730 mRNA. Translation: BAH19455.1.
PIRiT04952.
RefSeqiNP_001031686.1. NM_001036609.1. [O49562-2]
NP_193853.1. NM_118240.3. [O49562-1]
UniGeneiAt.20726.

Genome annotation databases

EnsemblPlantsiAT4G21210.1; AT4G21210.1; AT4G21210. [O49562-1]
GeneIDi827869.
KEGGiath:AT4G21210.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021960 Genomic DNA. Translation: CAA17540.1.
AL161554 Genomic DNA. Translation: CAB79121.1.
CP002687 Genomic DNA. Translation: AEE84423.1.
CP002687 Genomic DNA. Translation: AEE84424.1.
AK316730 mRNA. Translation: BAH19455.1.
PIRiT04952.
RefSeqiNP_001031686.1. NM_001036609.1. [O49562-2]
NP_193853.1. NM_118240.3. [O49562-1]
UniGeneiAt.20726.

3D structure databases

ProteinModelPortaliO49562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G21210.1.

Proteomic databases

PaxDbiO49562.
PRIDEiO49562.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G21210.1; AT4G21210.1; AT4G21210. [O49562-1]
GeneIDi827869.
KEGGiath:AT4G21210.

Organism-specific databases

TAIRiAT4G21210.

Phylogenomic databases

eggNOGiENOG410IFEV. Eukaryota.
COG1806. LUCA.
HOGENOMiHOG000218052.
InParanoidiO49562.
KOiK20115.
OMAiNRAMPRI.
PhylomeDBiO49562.

Enzyme and pathway databases

BRENDAi2.7.11.32. 399.
2.7.4.27. 399.

Miscellaneous databases

PROiO49562.

Gene expression databases

ExpressionAtlasiO49562. baseline and differential.
GenevisibleiO49562. AT.

Family and domain databases

HAMAPiMF_00921. PDRP.
InterProiIPR005177. Kinase-pyrophosphorylase.
IPR026565. PPDK_reg.
IPR017409. Pyrv_Pi_dikinase_reg_chlpt.
[Graphical view]
PfamiPF03618. Kinase-PPPase. 1 hit.
[Graphical view]
PIRSFiPIRSF038149. Pyruvate_Pi_dikinase_regulator. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure."
    Chastain C.J., Xu W., Parsley K., Sarath G., Hibberd J.M., Chollet R.
    Plant J. 53:854-863(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis are both bifunctional and interact with the catalytic and nucleotide-binding domains of pyruvate, orthophosphate dikinase."
    Astley H.M., Parsley K., Aubry S., Chastain C.J., Burnell J.N., Webb M.E., Hibberd J.M.
    Plant J. 68:1070-1080(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PPDK1, MUTAGENESIS OF SER-122; ASP-123; TYR-238; ASP-252; GLY-269; SER-271; ARG-272; LYS-275; PRO-277; SER-279; ALA-283; ASN-291; PRO-293; ARG-326; ARG-329; TYR-343; GLU-352; GLU-377; GLU-378; THR-379 AND ALA-380.

Entry informationi

Entry nameiPDRP1_ARATH
AccessioniPrimary (citable) accession number: O49562
Secondary accession number(s): B9DFD8, Q2V3G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The initial 51 amino acids are sufficient to act as a chloroplast transit peptide and the removal of the next 35 amino acids reduces the strength of interaction with PPDK significantly, which suggested that these residues are important for binding RP1 and may not be part of the transit peptide (PubMed:21883547).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.