PDRP2_ARATH
ID PDRP2_ARATH Reviewed; 377 AA.
AC Q9MAC9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pyruvate, phosphate dikinase regulatory protein 2;
DE EC=2.7.11.32 {ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:21883547};
DE EC=2.7.4.27 {ECO:0000269|PubMed:21883547};
DE AltName: Full=Pyruvate, Pi dikinase regulatory protein 2;
DE Short=AtRP2;
DE Short=PPDK RP2;
DE Short=PPDK regulatory protein 2;
GN Name=RP2; OrderedLocusNames=At3g01200; ORFNames=T4P13.11;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21414960; DOI=10.1093/jxb/err058;
RA Chastain C.J., Failing C.J., Manandhar L., Zimmerman M.A., Lakner M.M.,
RA Nguyen T.H.;
RT "Functional evolution of C(4) pyruvate, orthophosphate dikinase.";
RL J. Exp. Bot. 62:3083-3091(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PPDK1.
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. Has a much lower
CC phosphotransferase activity than PDRP1 (PubMed:21883547). Can use ADP
CC as a high specificity substrate and GDP as a lower affinity substrate,
CC but has no activity with UDP (PubMed:21414960).
CC {ECO:0000269|PubMed:17996018, ECO:0000269|PubMed:21414960,
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:21414960,
CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for ADP (at pH 6.8) {ECO:0000269|PubMed:21414960};
CC -!- SUBUNIT: Interacts with PPDK1. {ECO:0000269|PubMed:21883547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17996018}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen and seeds.
CC {ECO:0000269|PubMed:17996018}.
CC -!- MISCELLANEOUS: Was thought to be devoided of phosphorylase activity
CC (PubMed:17996018), but possess a much slower rate of phosphotransferase
CC than PDRP1. {ECO:0000269|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; AC008261; AAF26154.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73624.1; -; Genomic_DNA.
DR EMBL; BX822879; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_186769.1; NM_110986.4.
DR AlphaFoldDB; Q9MAC9; -.
DR SMR; Q9MAC9; -.
DR STRING; 3702.AT3G01200.1; -.
DR iPTMnet; Q9MAC9; -.
DR PaxDb; Q9MAC9; -.
DR PRIDE; Q9MAC9; -.
DR ProteomicsDB; 251327; -.
DR EnsemblPlants; AT3G01200.1; AT3G01200.1; AT3G01200.
DR GeneID; 821293; -.
DR Gramene; AT3G01200.1; AT3G01200.1; AT3G01200.
DR KEGG; ath:AT3G01200; -.
DR Araport; AT3G01200; -.
DR TAIR; locus:2102077; AT3G01200.
DR eggNOG; ENOG502QQ1R; Eukaryota.
DR HOGENOM; CLU_046206_0_0_1; -.
DR InParanoid; Q9MAC9; -.
DR OMA; AKEGAMC; -.
DR OrthoDB; 1388649at2759; -.
DR PhylomeDB; Q9MAC9; -.
DR BRENDA; 2.7.11.32; 399.
DR PRO; PR:Q9MAC9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MAC9; baseline and differential.
DR Genevisible; Q9MAC9; AT.
DR GO; GO:0009507; C:chloroplast; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..377
FT /note="Pyruvate, phosphate dikinase regulatory protein 2"
FT /id="PRO_0000342599"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 242..249
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255"
SQ SEQUENCE 377 AA; 41386 MW; 39150D70945FA302 CRC64;
MNLHGVSGHH EPNSEPPIPT GSSSPKLKIS PKLNRWSRGR ALRSGVKLDR PIPRSDNSPR
RQVTEAQPTD EADKKTTAID VEVTAGKSIY LVSDGTGWTA EHSVNAALGQ FEDFSLNRGS
SVNTHLFSWV EDEERLIEII KQAAKEGAMC FYTLANPSMA KSAKQACDQL GVLSVDILGP
IIEGIASHLG VSPSGLTRGA PGRVKTLNDA YFKRIEAIEF TIKQDDGTLP ENLSKADIVL
VGVSRTGKTP LSTYIAQKGY KVANVPFVMG VEPPRTLFQV EPRKVFGLKI QLVVLQAIRR
TRVKTLGVDT EAENNYSGID LVRKELDFAS RIYERNPGWA VIDVTNKAIE ETAAVILRLY
HDGRDTSTTV PRISKRY
