PPDK_FLAPR
ID PPDK_FLAPR Reviewed; 956 AA.
AC Q42736;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=PPDK; Synonyms=PDK;
OS Flaveria pringlei.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Tageteae; Flaveria.
OX NCBI_TaxID=4226;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=7948930; DOI=10.1007/bf00013761;
RA Rosche E., Streubel M., Westhoff P.;
RT "Primary structure of the photosynthetic pyruvate orthophosphate dikinase
RT of the C3 plant Flaveria pringlei and expression analysis of pyruvate
RT orthophosphate dikinase sequences in C3, C3-C4 and C4 Flaveria species.";
RL Plant Mol. Biol. 26:763-769(1994).
RN [2]
RP PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX PubMed=11950985; DOI=10.1104/pp.010806;
RA Chastain C.J., Fries J.P., Vogel J.A., Randklev C.L., Vossen A.P.,
RA Dittmer S.K., Watkins E.E., Fiedler L.J., Wacker S.A., Meinhover K.C.,
RA Sarath G., Chollet R.;
RT "Pyruvate,orthophosphate dikinase in leaves and chloroplasts of C(3) plants
RT undergoes light-/dark-induced reversible phosphorylation.";
RL Plant Physiol. 128:1368-1378(2002).
CC -!- FUNCTION: Formation of phosphoenolpyruvate.
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. {ECO:0000269|PubMed:11950985}.
CC -!- SUBUNIT: Homotetramer. {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-536 in the dark inactivates the enzyme.
CC Dephosphorylation upon light stimulation reactivates the enzyme.
CC {ECO:0000269|PubMed:11950985}.
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 -!- MISCELLANEOUS: A short cytoplasmic isoform may be produced by
CC alternative promoter usage. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; X75516; CAA53223.1; -; mRNA.
DR PIR; S53297; S53297.
DR PDB; 5JVN; X-ray; 2.90 A; A=83-956.
DR PDBsum; 5JVN; -.
DR AlphaFoldDB; Q42736; -.
DR SMR; Q42736; -.
DR PRIDE; Q42736; -.
DR BRENDA; 2.7.9.1; 2269.
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; 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 3D-structure; ATP-binding; Chloroplast; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Photosynthesis; Plastid; Transferase;
KW Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 80..956
FT /note="Pyruvate, phosphate dikinase, chloroplastic"
FT /id="PRO_0000023561"
FT ACT_SITE 538
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT ACT_SITE 916
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 644
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 701
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 830
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 830
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 851
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 852
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 853
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 854
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 854
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT MOD_RES 536
FT /note="Phosphothreonine; by PDRP1"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 257..275
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 382..399
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 426..438
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 444..448
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 453..459
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 485..493
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 494..502
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 538..546
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 561..564
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 602..614
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 626..634
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 639..644
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 653..663
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 668..692
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 707..710
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 716..727
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 731..741
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 746..748
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 753..758
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 760..779
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 785..790
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 796..817
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 824..829
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 832..836
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 838..842
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 846..850
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 852..860
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 867..869
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 871..876
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 884..886
FT /evidence="ECO:0007829|PDB:5JVN"
FT TURN 890..892
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 893..907
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 912..915
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 918..921
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 923..931
FT /evidence="ECO:0007829|PDB:5JVN"
FT STRAND 935..939
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 941..943
FT /evidence="ECO:0007829|PDB:5JVN"
FT HELIX 944..953
FT /evidence="ECO:0007829|PDB:5JVN"
SQ SEQUENCE 956 AA; 104554 MW; D7AF035937B4C2A8 CRC64;
MMSSLFVEGM LLKSADESCL PAKGKQRRTG DLRRLNHHRQ PAFVRWICRR KLSGVSRIEF
HSGGLTPPRA VLNPVSPPVT TTKKRVFTFG KGRSEGNKDM KSLLGGKGAN LAEMASIGLS
VPPGLTISTE ACEEYQQNGK KLPPGLWDEI LEGLRYVQKE MSASLGDPSK PLLLSVRSGA
AISMPGMMDT VLNLGLNDEV VAGLAGKSGA RFAYDSYRRF LDMFGNVVMG IPHSLFDEKL
EEMKAEKGVH LDTDLTAADL KDLVEQYKNV YVEAKGEKFP TDPKKQLELA VNAVFDSWDS
PRANKYRSIN QITGLKGTAV NIQCMVFGNM GNTSGTGVLF TRNPSTGEKK LYGEFLVNAQ
GEDVVAGIRT PEDLATMETC MPEAYRELVE NCKILERHYK DMMDIEFTVQ ENRLWMLQCR
TGKRTGKGAV RIAVDMVNEG LIDTRTAIKR VETQHLDQLL HPQFENPSAY KSHVVATGLP
ASPGAAVGQV VFSAEDAETW HAQGKSAILV RTETSPEDVG GMHAAAGILT ARGGMTSHAA
VVARGWGKCC VSGCADIRVN DDMKVLTIGD RVIKEGDWLS LNGSTGEVIL GKQLLAPPAM
SNDLETFMSW ADQVRRLKVM ANADTPNDAL TARNNGAQGI GLCRTEHMFF ASDERIKAVR
KMIMAVTPEQ RKAALDLLLP YQRSDFEGIF RAMDGLPVTI RLLDPPLHEF LPEGDLEHIV
NELAVDTGMS EDEIYSKIEK LSEVNPMLGF RGCRLGISYP ELTEMQVRAI FQAAVSMNNQ
GVTVIPEIMV PLVGTPQELR HQIGVIRGVA ANVFAEMGLT MDYKVGTMIE IPRAALIAEE
IAKEAEFFSF GTNDLTQMTF GYSRDDVGKF LQIYLSQGIL QHDPFEVLDQ KGVGQLIKMA
TEKGRAANPN LKVGICGEHG GEPSSVAFFD GVGLDYVSCS PFRVPIARLA AAQVVV
