PDRP1_MAIZE
ID PDRP1_MAIZE Reviewed; 426 AA.
AC Q195N6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Pyruvate, phosphate dikinase regulatory protein, chloroplastic;
DE EC=2.7.11.32 {ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:2983615};
DE EC=2.7.4.27 {ECO:0000269|PubMed:2983615};
DE AltName: Full=Bifunctional dikinase regulatory protein;
DE Short=BFRP;
DE AltName: Full=Pyruvate, Pi dikinase regulatory protein;
DE Short=PPDK RP;
DE Short=PPDK regulatory protein;
DE Flags: Precursor;
GN Name=PDRP1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], EXPRESSION, AND CHARACTERIZATION.
RC TISSUE=Leaf;
RX PubMed=16696949; DOI=10.1016/j.bbrc.2006.04.150;
RA Burnell J.N., Chastain C.J.;
RT "Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory
RT protein gene.";
RL Biochem. Biophys. Res. Commun. 345:675-680(2006).
RN [2]
RP FUNCTION.
RX PubMed=6326674; DOI=10.1016/0003-9861(84)90375-8;
RA Burnell J.N., Hatch M.D.;
RT "Regulation of C4 photosynthesis: identification of a catalytically
RT important histidine residue and its role in the regulation of pyruvate,Pi
RT dikinase.";
RL Arch. Biochem. Biophys. 231:175-182(1984).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=2983615; DOI=10.1016/0003-9861(85)90302-9;
RA Burnell J.N., Hatch M.D.;
RT "Regulation of C4 photosynthesis: purification and properties of the
RT protein catalyzing ADP-mediated inactivation and Pi-mediated activation of
RT pyruvate,Pi dikinase.";
RL Arch. Biochem. Biophys. 237:490-503(1985).
RN [4]
RP FUNCTION.
RX PubMed=2834385; DOI=10.1016/s0021-9258(18)68696-x;
RA Roeske C.A., Kutny R.M., Budde R.J.A., Chollet R.;
RT "Sequence of the phosphothreonyl regulatory site peptide from inactive
RT maize leaf pyruvate, orthophosphate dikinase.";
RL J. Biol. Chem. 263:6683-6687(1988).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=8311453; DOI=10.1006/abbi.1994.1028;
RA Smith C.M., Duff S.M., Chollet R.;
RT "Partial purification and characterization of maize-leaf pyruvate,
RT orthophosphate dikinase regulatory protein: a low-abundance, mesophyll-
RT chloroplast stromal protein.";
RL Arch. Biochem. Biophys. 308:200-206(1994).
RN [6]
RP FUNCTION.
RX PubMed=10683263; DOI=10.1006/abbi.1999.1651;
RA Chastain C.J., Botschner M., Harrington G.E., Thompson B.J., Mills S.E.,
RA Sarath G., Chollet R.;
RT "Further analysis of maize C(4) pyruvate,orthophosphate dikinase
RT phosphorylation by its bifunctional regulatory protein using selective
RT substitutions of the regulatory Thr-456 and catalytic His-458 residues.";
RL Arch. Biochem. Biophys. 375:165-170(2000).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=24710069; DOI=10.1104/pp.113.231993;
RA Chen Y.B., Lu T.C., Wang H.X., Shen J., Bu T.T., Chao Q., Gao Z.F.,
RA Zhu X.G., Wang Y.F., Wang B.C.;
RT "Posttranslational modification of maize chloroplast pyruvate
RT orthophosphate dikinase reveals the precise regulatory mechanism of its
RT enzymatic activity.";
RL Plant Physiol. 165:534-549(2014).
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 Phosphorylates PPDK at both Ser-528 and Thr-527 (PubMed:24710069). Can
CC use ADP as a high specificity substrate and GDP as a lower affinity
CC substrate, but has no activity with UDP (PubMed:21414960).
CC {ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:21414960,
CC ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:2834385,
CC ECO:0000269|PubMed:6326674}.
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:2983615};
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:2983615};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:2983615};
CC -!- ACTIVITY REGULATION: Regulated by light/dark exposure.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52 uM for ADP {ECO:0000269|PubMed:2983615};
CC KM=1.2 uM for [pyruvate, phosphate dikinase]
CC {ECO:0000269|PubMed:2983615};
CC KM=0.7 mM for phosphate {ECO:0000269|PubMed:2983615};
CC KM=0.7 uM for [Pyruvate, phosphate dikinase] phosphate
CC {ECO:0000269|PubMed:2983615};
CC pH dependence:
CC Optimum pH is 7.8-8.4 for both catalytic activities.
CC {ECO:0000269|PubMed:2983615};
CC -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- SUBUNIT: homodimer at pH 7.5 and homotetramer at pH 8.3.
CC {ECO:0000269|PubMed:2983615}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:8311453}.
CC -!- TISSUE SPECIFICITY: Leaf mesophyll-cells.
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PDRP subfamily. {ECO:0000305}.
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DR EMBL; DQ645424; ABG00151.1; -; mRNA.
DR PDB; 5D0N; X-ray; 3.20 A; A=38-426.
DR PDB; 5D1F; X-ray; 3.40 A; A=38-426.
DR PDBsum; 5D0N; -.
DR PDBsum; 5D1F; -.
DR AlphaFoldDB; Q195N6; -.
DR SMR; Q195N6; -.
DR STRING; 4577.GRMZM2G131286_P01; -.
DR PaxDb; Q195N6; -.
DR PRIDE; Q195N6; -.
DR MaizeGDB; 293064; -.
DR eggNOG; ENOG502QQ1R; Eukaryota.
DR BRENDA; 2.7.4.27; 6752.
DR UniPathway; UPA00322; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q195N6; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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: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 3D-structure; Chloroplast; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..426
FT /note="Pyruvate, phosphate dikinase regulatory protein,
FT chloroplastic"
FT /id="PRO_0000315393"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153..160
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:5D0N"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:5D0N"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:5D0N"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:5D0N"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:5D1F"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5D1F"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:5D0N"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:5D0N"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:5D1F"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 371..385
FT /evidence="ECO:0007829|PDB:5D0N"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:5D0N"
FT HELIX 399..414
FT /evidence="ECO:0007829|PDB:5D0N"
SQ SEQUENCE 426 AA; 45905 MW; 99F6F7B2B0D9F6D6 CRC64;
MIGCAKPLAA PLQAWARPPS PAGRRLPPSF CAPDTSPALT RAVESPGQSQ SDDAPPPRSG
EAASSLAPRA SSHLDRWSRS RALRSGHRPA LNRAALSSAS VSAPPVIKSP RPEDAAVAAE
DGEDDDVCEA ERDAAAGKAI YIVSDGTGWT AEHSVNAALG QFENCLADRG CAVNTHLFSL
IDDMDRLIEV IKQAAKEGAL VLYTLADPSM AEATKKACDF WGVPCTDVLR PTVEAIASHI
GVAPSGIPRS FPSRNGRLSE DYFQRIDAID FTIKQDDGVL PQNFYRADIV LAGVSRTGKT
PLSIYLAQKG YKVANVPIVM GVALPKSLFE INQDKVFGLT INPAILQGIR KTRAKTLGFD
GRQSNYAEMD HVRQELVHAN QIFVQNPWWP VIAVTGKAIE ETAAVILGIL HDRKQKCSMP
RISKRY
