ID PPDK_MESCR Reviewed; 949 AA.
AC Q42910; Q42911;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 119.
DE RecName: Full=Pyruvate, phosphate dikinase, chloroplastic;
DE EC=2.7.9.1 {ECO:0000250|UniProtKB:P11155};
DE AltName: Full=Pyruvate, orthophosphate dikinase;
DE Flags: Precursor;
GN Name=PPD; Synonyms=PPDK;
OS Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Aizoaceae; Mesembryanthemum;
OC Mesembryanthemum subgen. Cryophytum.
OX NCBI_TaxID=3544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=7647683; DOI=10.1007/bf00203649;
RA Fisslthaler B., Meyer G., Bohnert H.J., Schmitt J.M.;
RT "Age-dependent induction of pyruvate, orthophosphate dikinase in
RT Mesembryanthemum crystallinum L.";
RL Planta 196:492-500(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Fisslthaler B., Meyer G., Schmitt J.M.;
RT "The gene encoding pyruvate, orthophosphate dikinase from Mesembryanthemum
RT crystallinum L. has a long intron in the 5' untranslated region.";
RL (er) Plant Gene Register PGR96-010(1996).
CC -!- FUNCTION: Formation of phosphoenolpyruvate, which is the primary
CC acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants.
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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. {ECO:0000250}.
CC -!- PTM: Phosphorylation of Thr-530 in the dark inactivates the enzyme.
CC Dephosphorylation upon light stimulation reactivates the enzyme (By
CC similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; X78347; CAA55143.1; -; mRNA.
DR EMBL; X82489; CAA57872.1; -; Genomic_DNA.
DR PIR; S55478; S55478.
DR AlphaFoldDB; Q42910; -.
DR SMR; Q42910; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 1.20.80.30; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 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 NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Photosynthesis; Plastid; Transferase;
KW Transit peptide.
FT TRANSIT 1..74
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 75..949
FT /note="Pyruvate, phosphate dikinase, chloroplastic"
FT /id="PRO_0000023564"
FT ACT_SITE 532
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT ACT_SITE 910
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 638
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 695
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 824
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 824
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 845
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 846
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 847
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 848
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 848
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT MOD_RES 530
FT /note="Phosphothreonine; by PDRP1"
FT /evidence="ECO:0000250"
FT CONFLICT 240
FT /note="A -> V (in Ref. 1; CAA55143)"
FT /evidence="ECO:0000305"
FT CONFLICT 582..589
FT /note="VILGKVPL -> SYLRESTT (in Ref. 1; CAA55143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 949 AA; 103084 MW; 006D7C0D47E83D48 CRC64;
MASAFKGILI RSPPDVCAET VAKVSQCNRA QLVKNSSTGF KNIFKLSEAR KFHAPVASHL
RSQAVMAPAS DPTSTAIKRV FTFGKGRSEG NKGMKSLLGG KGANLAEMAS IGLSVPPGLT
ISTEACQEYQ EHGKQLSAGL WEEILEGLRV IEKDMGSYLG DPSKPLLLSV RSGAAISMPG
MMDTVLNLGL NDDVVAGLAA KSGERFAYDS YRRFLDMFGN VVMGISHSSF EEKLEKLKQA
KGVKLDTELT ASDLKEVVEQ YKNVYLEVKG EKFPADPERQ LQLAIQAVFD SWDSPRAIKY
RNINQITGLK GTAVNIQCMV FGNMGNTSGT GVLFTRNPST GEKKLYGEFL INAQGEDVVA
GIRTPEDLDT MRSCMPEAYK ELVENCEILE RHYKDMMDIE FTVQENRLWM LQCRSGKRTG
KGAVKIAVDL VKEGIVDTYT AIKMVEPQHL DQLLHPQFED PSAYKDRVIA TGLPASPGAA
VGQIIFSADE AESWQAQGKS VILVRNETSP EDVGGMHAAI GILTARGGMT SHAAVVAGGW
GKCCVSGCSE IRVNDTDKVL LVGDKVISEG DWLSLNGSTG EVILGKVPLS PPALSGDLET
FMSWADDIRV LKVMANADTP EDALAARNNG AEGIGLCRTE HMFFASDDRI KTVRKMIMAV
TSEQRKVALD QLLPYQRSDF EGIFRAMDGL PVTIRLLDPP LHEFLPEGDV EQIVSELTLE
TGMAEDEIFS RIEKLSEVNP MLGFRGCRLG ISYPELTEMQ ARAIFQAAVS MSNQGVKVFP
EIMVPLVGTP QELGHQVSLI RNVAEKVFSE TGSSLSYKVG TMIEIPRAAL VADEIAMEAE
FFSFGTNDLT QMTFGYSRDD VGKFLPVYLS KGILQSDPFE VLDQKGVGQL IKLATEKGRS
ARPSLKVGIC GEHGGEPSSV AFFAEAGLDY VSCSPFRVPI ARLAAAQVV
//
