PPDK1_ARATH
ID PPDK1_ARATH Reviewed; 963 AA.
AC O23404; B9DGK5; Q27GJ5; Q2V3I1; Q3EA16;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Pyruvate, phosphate dikinase 1, chloroplastic;
DE EC=2.7.9.1;
DE AltName: Full=Pyruvate, orthophosphate dikinase 1;
DE Flags: Precursor;
GN Name=PPDK; OrderedLocusNames=At4g15530; ORFNames=dl3805c, FCAALL.325;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE
RP PROMOTER USAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=16915520; DOI=10.1007/s11103-006-9023-0;
RA Parsley K., Hibberd J.M.;
RT "The Arabidopsis PPDK gene is transcribed from two promoters to produce
RT differentially expressed transcripts responsible for cytosolic and
RT plastidic proteins.";
RL Plant Mol. Biol. 62:339-349(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=15272878; DOI=10.1111/j.1365-313x.2004.02160.x;
RA Lin J.F., Wu S.H.;
RT "Molecular events in senescing Arabidopsis leaves.";
RL Plant J. 39:612-628(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
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 [12]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-543, INTERACTION WITH RP1
RP AND RP2, AND DOMAIN.
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).
RN [13]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-76, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Formation of phosphoenolpyruvate. May be involved in
CC regulating the flux of carbon into starch and fatty acids of seeds and
CC in the remobilization of nitrogen reserves in senescing leaves.
CC {ECO:0000269|PubMed:15272878, ECO:0000269|PubMed:16915520,
CC ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:21883547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC Evidence={ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:21883547};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P11155};
CC -!- ACTIVITY REGULATION: Activated by light-induced dephosphorylation.
CC Inhibited by dark-induced phosphorylation. Both reactions are catalyzed
CC by PDRP1. {ECO:0000250|UniProtKB:P11155}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for pyruvate {ECO:0000269|PubMed:21414960};
CC KM=292 uM for phosphoenolpyruvate {ECO:0000269|PubMed:21414960};
CC -!- SUBUNIT: Homotetramer. Interacts with RP1 and RP2.
CC {ECO:0000250|UniProtKB:P11155, ECO:0000269|PubMed:21883547}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16915520}. Cytoplasm {ECO:0000269|PubMed:16915520}.
CC Note=Isoform 1 is targeted to the chloroplast while isoform 2 is found
CC in the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Comment=One additional alternative promoter may be used. According to
CC EST data.;
CC Name=1;
CC IsoId=O23404-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O23404-2; Sequence=VSP_034604, VSP_034606;
CC Name=3;
CC IsoId=O23404-3; Sequence=VSP_034605;
CC Name=4;
CC IsoId=O23404-4; Sequence=VSP_034603;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in leaves, flowers and
CC siliques. Isoform 2 is found in cotyledons, rosette and cauline leaves,
CC petioles, flowers and siliques. {ECO:0000269|PubMed:16915520}.
CC -!- DEVELOPMENTAL STAGE: Both isoforms 1 and 2 increase up to 7 days after
CC sowing, but then decline. {ECO:0000269|PubMed:16915520}.
CC -!- INDUCTION: Isoform 2, but not isoform 1, is induced during darkness.
CC {ECO:0000269|PubMed:15272878, ECO:0000269|PubMed:16915520}.
CC -!- DOMAIN: The catalytic core domain alone is sufficient for the binding
CC to PDRP1 but not for the binding to PDRP2.
CC {ECO:0000269|PubMed:21883547}.
CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and the
CC C-terminal domain the pyruvate binding site.
CC {ECO:0000250|UniProtKB:P11155}.
CC -!- PTM: Phosphorylation of Thr-543 in the dark inactivates the enzyme.
CC Dephosphorylation upon light stimulation reactivates the enzyme.
CC {ECO:0000250|UniProtKB:P11155}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC phosphocarrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the N-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the C-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the N-terminal domain to that of the C-terminal domain.
CC {ECO:0000250|UniProtKB:P11155}.
CC -!- MISCELLANEOUS: [Isoform 1]: Translation of the sequence shown in
CC PubMed:16915520 was N-terminally extended.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC Cytoplasmic. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10331.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78595.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97339; CAB10331.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161541; CAB78595.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83616.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83617.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83618.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83619.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83620.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83621.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67012.1; -; Genomic_DNA.
DR EMBL; AK317187; BAH19872.1; -; mRNA.
DR PIR; A71420; A71420.
DR RefSeq; NP_001031647.1; NM_001036570.1. [O23404-4]
DR RefSeq; NP_001078395.1; NM_001084926.1. [O23404-3]
DR RefSeq; NP_001078396.1; NM_001084927.2. [O23404-1]
DR RefSeq; NP_001118987.1; NM_001125515.1. [O23404-1]
DR RefSeq; NP_001328869.1; NM_001341051.1. [O23404-4]
DR RefSeq; NP_193288.2; NM_117643.4. [O23404-2]
DR RefSeq; NP_849391.2; NM_179060.4. [O23404-3]
DR AlphaFoldDB; O23404; -.
DR SMR; O23404; -.
DR BioGRID; 12523; 4.
DR STRING; 3702.AT4G15530.5; -.
DR iPTMnet; O23404; -.
DR PaxDb; O23404; -.
DR PRIDE; O23404; -.
DR ProteomicsDB; 249342; -. [O23404-1]
DR EnsemblPlants; AT4G15530.1; AT4G15530.1; AT4G15530. [O23404-3]
DR EnsemblPlants; AT4G15530.2; AT4G15530.2; AT4G15530. [O23404-2]
DR EnsemblPlants; AT4G15530.3; AT4G15530.3; AT4G15530. [O23404-4]
DR EnsemblPlants; AT4G15530.4; AT4G15530.4; AT4G15530. [O23404-3]
DR EnsemblPlants; AT4G15530.5; AT4G15530.5; AT4G15530. [O23404-1]
DR EnsemblPlants; AT4G15530.6; AT4G15530.6; AT4G15530. [O23404-1]
DR EnsemblPlants; AT4G15530.7; AT4G15530.7; AT4G15530. [O23404-4]
DR GeneID; 827226; -.
DR Gramene; AT4G15530.1; AT4G15530.1; AT4G15530. [O23404-3]
DR Gramene; AT4G15530.2; AT4G15530.2; AT4G15530. [O23404-2]
DR Gramene; AT4G15530.3; AT4G15530.3; AT4G15530. [O23404-4]
DR Gramene; AT4G15530.4; AT4G15530.4; AT4G15530. [O23404-3]
DR Gramene; AT4G15530.5; AT4G15530.5; AT4G15530. [O23404-1]
DR Gramene; AT4G15530.6; AT4G15530.6; AT4G15530. [O23404-1]
DR Gramene; AT4G15530.7; AT4G15530.7; AT4G15530. [O23404-4]
DR KEGG; ath:AT4G15530; -.
DR Araport; AT4G15530; -.
DR TAIR; locus:2130324; AT4G15530.
DR eggNOG; ENOG502QREJ; Eukaryota.
DR InParanoid; O23404; -.
DR OrthoDB; 225519at2759; -.
DR PhylomeDB; O23404; -.
DR BioCyc; ARA:AT4G15530-MON; -.
DR BRENDA; 2.7.11.32; 399.
DR PRO; PR:O23404; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23404; baseline and differential.
DR Genevisible; O23404; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR22931; PTHR22931; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 3.
DR PIRSF; PIRSF000853; PPDK; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01828; pyru_phos_dikin; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; ATP-binding; Chloroplast;
KW Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Photosynthesis; Plastid; Pyruvate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 77..963
FT /note="Pyruvate, phosphate dikinase 1, chloroplastic"
FT /id="PRO_0000343515"
FT ACT_SITE 545
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT ACT_SITE 922
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 651
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 707
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250, ECO:0000250|UniProtKB:P11155"
FT BINDING 836
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 857
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 858
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 859
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 860
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 860
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT MOD_RES 543
FT /note="Phosphothreonine; by PDRP1"
FT /evidence="ECO:0007744|PubMed:18433157"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_034603"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16915520"
FT /id="VSP_034604"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_034605"
FT VAR_SEQ 89..91
FT /note="AQK -> MMQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16915520"
FT /id="VSP_034606"
FT MUTAGEN 543
FT /note="T->D: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:21883547"
SQ SEQUENCE 963 AA; 105138 MW; 239263180A836FE2 CRC64;
MLYIRKKMTS MIVKTTPELF KGNGVFRTDH LGENRMVSRS NRLGDGSNRF PRTGTIHCQR
LSIAKTGLHR ETKARAILSP VSDPAASIAQ KRVFTFGKGR SEGNKGMKSL LGGKGANLAE
MASIGLSVPP GLTISTEACQ QYQIAGKKLP EGLWEEILEG LSFIERDIGA SLADPSKPLL
LSVRSGAAIS MPGMMDTVLN LGLNDQVVVG LAAKSGERFA YDSFRRFLDM FGDVVMGIPH
AKFEEKLERM KERKGVKNDT DLSAADLKEL VEQYKSVYLE AKGQEFPSDP KKQLELAIEA
VFDSWDSPRA NKYRSINQIT GLKGTAVNIQ CMVFGNMGDT SGTGVLFTRN PSTGEKKLYG
EFLVNAQGED VVAGIRTPED LDTMKRFMPE AYAELVENCN ILERHYKDMM DIEFTVQEER
LWMLQCRAGK RTGKGAVKIA VDMVGEGLVE KSSAIKMVEP QHLDQLLHPQ FHDPSGYREK
VVAKGLPASP GAAVGQVVFT AEEAEAWHSQ GKTVILVRTE TSPDDVGGMH AAEGILTARG
GMTSHAAVVA RGWGKCCIAG CSEIRVDENH KVLLIGDLTI NEGEWISMNG STGEVILGKQ
ALAPPALSPD LETFMSWADA IRRLKVMANA DTPEDAIAAR KNGAQGIGLC RTEHMFFGAD
RIKAVRKMIM AVTTEQRKAS LDILLPYQRS DFEGIFRAMD GLPVTIRLLD PPLHEFLPEG
DLDNIVHELA EETGVKEDEV LSRIEKLSEV NPMLGFRGCR LGISYPELTE MQARAIFEAA
ASMQDQGVTV IPEIMVPLVG TPQELGHQVD VIRKVAKKVF AEKGHTVSYK VGTMIEIPRA
ALIADEIAKE AEFFSFGTND LTQMTFGYSR DDVGKFLPIY LAKGILQHDP FEVLDQQGVG
QLIKMATEKG RAARPSLKVG ICGEHGGDPS SVGFFAEAGL DYVSCSPFRV PIARLAAAQV
VVA
