PDRP1_ARATH
ID PDRP1_ARATH Reviewed; 403 AA.
AC O49562; B9DFD8; Q2V3G6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic;
DE EC=2.7.11.32 {ECO:0000269|PubMed:21883547};
DE EC=2.7.4.27 {ECO:0000269|PubMed:21883547};
DE AltName: Full=Bifunctional dikinase regulatory protein 1;
DE Short=AtRP1;
DE Short=BFRP1;
DE AltName: Full=Pyruvate, Pi dikinase regulatory protein 1;
DE Short=PPDK RP1;
DE Short=PPDK regulatory protein 1;
DE Flags: Precursor;
GN Name=RP1; OrderedLocusNames=At4g21210; ORFNames=F7J7.150;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17996018; DOI=10.1111/j.1365-313x.2007.03366.x;
RA Chastain C.J., Xu W., Parsley K., Sarath G., Hibberd J.M., Chollet R.;
RT "The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis
RT possess a novel, unprecedented Ser/Thr protein kinase primary structure.";
RL Plant J. 53:854-863(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PPDK1, AND MUTAGENESIS OF
RP SER-122; ASP-123; TYR-238; ASP-252; GLY-269; SER-271; ARG-272; LYS-275;
RP PRO-277; SER-279; ALA-283; ASN-291; PRO-293; ARG-326; ARG-329; TYR-343;
RP GLU-352; GLU-377; GLU-378; THR-379 AND ALA-380.
RX PubMed=21883547; DOI=10.1111/j.1365-313x.2011.04759.x;
RA Astley H.M., Parsley K., Aubry S., Chastain C.J., Burnell J.N., Webb M.E.,
RA Hibberd J.M.;
RT "The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis
RT are both bifunctional and interact with the catalytic and nucleotide-
RT binding domains of pyruvate, orthophosphate dikinase.";
RL Plant J. 68:1070-1080(2011).
CC -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC involved in the dark/light-mediated regulation of PPDK by catalyzing
CC its phosphorylation/dephosphorylation. Dark/light-induced changes in
CC stromal concentrations of the competing ADP and Pi substrates govern
CC the direction of the reaction. In the dark, phosphorylates the
CC catalytic intermediate of PPDK (PPDK-HisP), inactivating it. Light
CC exposure induces the phosphorolysis reaction that reactivates PPDK.
CC Unlike the kinase function which can utilize either Thr or Ser as
CC target, the phosphorylase function has a strict substrate requirement
CC for threonyl phosphate. {ECO:0000269|PubMed:17996018,
CC ECO:0000269|PubMed:21883547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate,
CC phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-
CC phospho-L-threonyl-[pyruvate, phosphate dikinase];
CC Xref=Rhea:RHEA:43692, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:83586, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.11.32; Evidence={ECO:0000269|PubMed:21883547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-
CC [pyruvate, phosphate dikinase] + phosphate = diphosphate + N(tele)-
CC phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase];
CC Xref=Rhea:RHEA:43696, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61977, ChEBI:CHEBI:83586; EC=2.7.4.27;
CC Evidence={ECO:0000269|PubMed:21883547};
CC -!- ACTIVITY REGULATION: Regulated by light/dark exposure.
CC -!- SUBUNIT: Interacts with PPDK1. {ECO:0000269|PubMed:21883547}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:17996018}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O49562-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O49562-2; Sequence=VSP_034504;
CC -!- TISSUE SPECIFICITY: Expressed in green tissues.
CC {ECO:0000269|PubMed:17996018}.
CC -!- MISCELLANEOUS: The initial 51 amino acids are sufficient to act as a
CC chloroplast transit peptide and the removal of the next 35 amino acids
CC reduces the strength of interaction with PPDK significantly, which
CC suggested that these residues are important for binding RP1 and may not
CC be part of the transit peptide (PubMed:21883547).
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PDRP subfamily. {ECO:0000305}.
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DR EMBL; AL021960; CAA17540.1; -; Genomic_DNA.
DR EMBL; AL161554; CAB79121.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84423.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84424.1; -; Genomic_DNA.
DR EMBL; AK316730; BAH19455.1; -; mRNA.
DR PIR; T04952; T04952.
DR RefSeq; NP_001031686.1; NM_001036609.1. [O49562-2]
DR RefSeq; NP_193853.1; NM_118240.4. [O49562-1]
DR AlphaFoldDB; O49562; -.
DR SMR; O49562; -.
DR IntAct; O49562; 1.
DR STRING; 3702.AT4G21210.1; -.
DR PaxDb; O49562; -.
DR PRIDE; O49562; -.
DR ProteomicsDB; 251349; -. [O49562-1]
DR EnsemblPlants; AT4G21210.1; AT4G21210.1; AT4G21210. [O49562-1]
DR EnsemblPlants; AT4G21210.2; AT4G21210.2; AT4G21210. [O49562-2]
DR GeneID; 827869; -.
DR Gramene; AT4G21210.1; AT4G21210.1; AT4G21210. [O49562-1]
DR Gramene; AT4G21210.2; AT4G21210.2; AT4G21210. [O49562-2]
DR KEGG; ath:AT4G21210; -.
DR Araport; AT4G21210; -.
DR TAIR; locus:2127413; AT4G21210.
DR eggNOG; ENOG502SAAN; Eukaryota.
DR HOGENOM; CLU_046206_0_0_1; -.
DR InParanoid; O49562; -.
DR OMA; YAQCEFE; -.
DR OrthoDB; 1388649at2759; -.
DR PhylomeDB; O49562; -.
DR BRENDA; 2.7.11.32; 399.
DR BRENDA; 2.7.4.27; 399.
DR PRO; PR:O49562; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49562; baseline and differential.
DR Genevisible; O49562; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_00921; PDRP; 1.
DR InterPro; IPR005177; Kinase-pyrophosphorylase.
DR InterPro; IPR026565; PPDK_reg.
DR InterPro; IPR017409; Pyrv_Pi_dikinase_reg_chlpt.
DR PANTHER; PTHR31756; PTHR31756; 1.
DR Pfam; PF03618; Kinase-PPPase; 1.
DR PIRSF; PIRSF038149; Pyruvate_Pi_dikinase_regulator; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transit peptide.
FT TRANSIT 1..86
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 87..403
FT /note="Pyruvate, phosphate dikinase regulatory protein 1,
FT chloroplastic"
FT /id="PRO_0000196751"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 269..276
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255"
FT VAR_SEQ 297..323
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034504"
FT MUTAGEN 122
FT /note="S->A: No effect on phosphotransferase and kinase
FT activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 123
FT /note="D->A: No effect on phosphotransferase and kinase
FT activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 238
FT /note="Y->F: No effect on phosphotransferase and kinase
FT activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 252
FT /note="D->N: No effect on the interaction with PPDK, but
FT loss of phosphotransferase activity and partially reduced
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 269
FT /note="G->A: No effect on the interaction with PPDK, but
FT loss of phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 271
FT /note="S->A: No effect on the interaction with PPDK, but
FT loss of phosphotransferase activity and partially reduced
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 272
FT /note="R->M: Weak interaction with PPDK, and loss of
FT phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 275
FT /note="K->M: Weak interaction with PPDK, and loss of
FT phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 277
FT /note="P->A: Weak interaction with PPDK, and loss of
FT phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 279
FT /note="S->A: No effect on phosphotransferase and kinase
FT activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 283
FT /note="A->T: No effect on the interaction with PPDK, but
FT loss of phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 291
FT /note="N->A: No effect on the interaction with PPDK, but
FT loss of phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 293
FT /note="P->A: No effect on the interaction with PPDK, but
FT reduced phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 326
FT /note="R->M: Weak interaction with PPDK, and loss of
FT phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 329
FT /note="R->M: No effect on the interaction with PPDK, but
FT loss of phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 343
FT /note="Y->F: Weak effect on the interaction with PPDK, but
FT loss of phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 352
FT /note="E->Q: Weak interaction with PPDK, and loss of
FT phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 377
FT /note="E->Q: Weak interaction with PPDK, and loss of
FT phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 378
FT /note="E->Q: No effect on phosphotransferase and kinase
FT activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 379
FT /note="T->V: No effect on phosphotransferase and kinase
FT activities."
FT /evidence="ECO:0000269|PubMed:21883547"
FT MUTAGEN 380
FT /note="A->T: No effect on the interaction with PPDK, but
FT loss of phosphotransferase and kinase activities."
FT /evidence="ECO:0000269|PubMed:21883547"
SQ SEQUENCE 403 AA; 43684 MW; 125AF179D5EA6564 CRC64;
MALLSAMKLQ GRPPPISSNL NPNSKPAGSD SVSLNASEPG SERKPRKFSS QLNRWNRART
LRSGAKLDST ITNGSNNTTG PMRPIESSSR TDVSTLDSDV SSSSNGVSEA DMTAAKSIYI
VSDGTGWTAE HAVNAALGQF DYCLVDRGCP VNTHLFSGIE DGEKLMEIIK QAAREGAMVI
YTLADPSMAE ATMRACKLWK IPSLDILGPI TESISSHLGT NPSGLSRGIT NSSLNEDYFK
RIEAIEFTIK HDDGALPENL EKADIVLVGV SRTGKTPLST YLAQKGYKVS NVPIVNGVDL
PKTLFEIDPR KVFGLMINPL VLQGIREARA KSLGLGSSFK TKYSELGSVK EELELAKKIF
AENPTWPVIE VTESAIEETA AVVLRLYDER QSNRAMPRIS KSY
