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Pyruvate, phosphate dikinase, chloroplastic (EC 2.7.9.1) (Cold-sensitive pyruvate, orthophosphate dikinase) (Pyruvate, orthophosphate dikinase)

 PPDK_FLABI              Reviewed;         953 AA.
Q39735;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 110.
RecName: Full=Pyruvate, phosphate dikinase, chloroplastic;
EC=2.7.9.1;
AltName: Full=Cold-sensitive pyruvate, orthophosphate dikinase;
AltName: Full=Pyruvate, orthophosphate dikinase;
Flags: Precursor;
Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; campanulids; Asterales; Asteraceae;
Asteroideae; Heliantheae alliance; Tageteae; Flaveria.
NCBI_TaxID=4224;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 78-86.
TISSUE=Leaf;
PubMed=7766886; DOI=10.1007/BF00037024;
Usami S., Ohta S., Komari T., Burnell J.N.;
"Cold stability of pyruvate, orthophosphate dikinase of Flaveria
brownii.";
Plant Mol. Biol. 27:969-980(1995).
[2]
BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND MUTAGENESIS OF
GLN-869; ALA-873; ILE-885 AND ILE-952.
PubMed=9038349; DOI=10.1016/S0014-5793(97)00015-X;
Ohta S., Usami S., Ueki J., Kumashiro T., Komari T., Burnell J.N.;
"Identification of the amino acid residues responsible for cold
tolerance in Flaveria brownii pyruvate,orthophosphate dikinase.";
FEBS Lett. 403:5-9(1997).
-!- FUNCTION: Formation of phosphoenolpyruvate, which is the primary
acceptor of CO(2) in C4 and some Crassulacean acid metabolism
plants.
-!- CATALYTIC ACTIVITY: ATP + pyruvate + phosphate = AMP +
phosphoenolpyruvate + diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P11155};
-!- ACTIVITY REGULATION: Activated by light-induced dephosphorylation.
Inhibited by dark-induced phosphorylation. Both reactions are
catalyzed by PDRP1 (By similarity). Inactivated by cold due to the
dissociation of the homotetramer. {ECO:0000250,
ECO:0000269|PubMed:9038349}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=73 uM for pyruvate {ECO:0000269|PubMed:9038349};
KM=25 uM for ATP {ECO:0000269|PubMed:9038349};
KM=118 uM for phosphate {ECO:0000269|PubMed:9038349};
Temperature dependence:
Loss of activity below 10 degrees Celsius.
{ECO:0000269|PubMed:9038349};
-!- PATHWAY: Photosynthesis; C4 acid pathway.
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site,
the central domain the pyrophosphate/phosphate carrier histidine,
and the C-terminal domain the pyruvate binding site.
{ECO:0000250}.
-!- DOMAIN: The C-terminal domain (829-953) is involved in cold
sensitivity.
-!- PTM: Phosphorylation of Thr-533 in the dark inactivates the
enzyme. Dephosphorylation upon light stimulation reactivates the
enzyme (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The reaction takes place in three steps, mediated
by a phosphocarrier histidine residue located on the surface of
the central domain. The two first partial reactions are catalyzed
at an active site located on the N-terminal domain, and the third
partial reaction is catalyzed at an active site located on the C-
terminal domain. For catalytic turnover, the central domain
swivels from the concave surface of the N-terminal domain to that
of the C-terminal domain (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: A short cytoplasmic isoform may be produced by
alternative promoter usage. {ECO:0000250}.
-!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
{ECO:0000305}.
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EMBL; U08400; AAA86941.1; -; mRNA.
PIR; S56650; S56650.
ProteinModelPortal; Q39735; -.
SMR; Q39735; -.
PRIDE; Q39735; -.
BRENDA; 2.7.9.1; 2264.
SABIO-RK; Q39735; -.
UniPathway; UPA00322; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
Gene3D; 3.30.1490.20; -; 2.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR008279; PEP-util_enz_mobile_dom.
InterPro; IPR018274; PEP_util_AS.
InterPro; IPR000121; PEP_util_C.
InterPro; IPR023151; PEP_util_CS.
InterPro; IPR036637; Phosphohistidine_dom_sf.
InterPro; IPR002192; PPDK_PEP-bd.
InterPro; IPR010121; Pyruvate_phosphate_dikinase.
InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
PANTHER; PTHR22931:SF9; PTHR22931:SF9; 1.
Pfam; PF00391; PEP-utilizers; 1.
Pfam; PF02896; PEP-utilizers_C; 1.
Pfam; PF01326; PPDK_N; 2.
PIRSF; PIRSF000853; PPDK; 1.
SUPFAM; SSF51621; SSF51621; 1.
SUPFAM; SSF52009; SSF52009; 1.
TIGRFAMs; TIGR01828; pyru_phos_dikin; 1.
PROSITE; PS00742; PEP_ENZYMES_2; 1.
PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
1: Evidence at protein level;
ATP-binding; Chloroplast; Direct protein sequencing; Kinase;
Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
Photosynthesis; Plastid; Transferase; Transit peptide.
TRANSIT 1 77 Chloroplast.
{ECO:0000269|PubMed:7766886}.
CHAIN 78 953 Pyruvate, phosphate dikinase,
chloroplastic.
/FTId=PRO_0000023559.
ACT_SITE 535 535 Tele-phosphohistidine intermediate.
{ECO:0000250|UniProtKB:P11155}.
ACT_SITE 913 913 Proton donor.
{ECO:0000250|UniProtKB:P11155}.
METAL 827 827 Magnesium.
{ECO:0000250|UniProtKB:P11155}.
METAL 851 851 Magnesium.
{ECO:0000250|UniProtKB:P11155}.
BINDING 641 641 Substrate.
{ECO:0000250|UniProtKB:P11155}.
BINDING 698 698 Substrate.
{ECO:0000250|UniProtKB:P11155}.
BINDING 827 827 Substrate.
{ECO:0000250|UniProtKB:P11155}.
BINDING 848 848 Substrate; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P11155}.
BINDING 849 849 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P11155}.
BINDING 850 850 Substrate.
{ECO:0000250|UniProtKB:P11155}.
BINDING 851 851 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P11155}.
MOD_RES 533 533 Phosphothreonine; by PDRP1.
{ECO:0000250}.
MUTAGEN 869 869 Q->P: 60% activity in the cold. 60%
activity in the cold; when associated
with S-873. {ECO:0000269|PubMed:9038349}.
MUTAGEN 873 873 A->S: 10% activity in the cold. 60%
activity in the cold; when associated
with P-869. {ECO:0000269|PubMed:9038349}.
MUTAGEN 885 885 I->L: 50% activity in the cold. 65%
activity in the cold; when associated
with V-952. {ECO:0000269|PubMed:9038349}.
MUTAGEN 952 952 I->V: 25% activity in the cold. 65%
activity in the cold; when associated
with L-885. {ECO:0000269|PubMed:9038349}.
SEQUENCE 953 AA; 104002 MW; 7BEC5276C1C1DC4C CRC64;
MMSSLSVEGM LLKSARESCL PARVNQRRNG DLRRLNHHRQ SSFVRCLTPA RVSRPELRSS
GLTPPRAVLN PVSPPVTTAK KRVFTFGKGR SEGNRDMKSL LGGKGANLAE MSSIGLSVPP
GLTISTEACE EYQQNGKSLP PGLWDEISEG LDYVQKEMSA SLGDPSKPLP LSVRSGAAIS
MPGMMDTVLN LGLNDEVVAG LAGKSGARFA YDSYRRFLDM FGNVVMGIPH SLFDEKLEQM
KAEKGIHLDT DLTAADLKDL VEKYKNVYVE AKGEKFPTDP KKQLELAVNA VFDSWDSPRA
NKYRSINQIT GLKGTAVNIQ SMVFGNMGNT SGTGVLFTRN PSTGEKKLYG EFLINAQGED
VVAGIRTPED LGTMETCMPD AYKELVENCE ILEGHYKDMM DIEFTVQENR LWMLQCRTGK
RTGKGAVRIA VDMVNEWLID TRTAIKRVET QHLDQLLHPQ FEDPSAYKSH VVATGLPASP
GAAVGQVCFS AEDAETWHAQ GKSAILVRTE TSPEDVGGMH AAAGILTARG GMTSHAAVVA
RGWGKCCVSG CADIRVNDDM KIFTIGDRVI KEGDWLSLNG TTGEVILGKQ LLAPPAMSND
LEIFMSWADQ ARRLKVMANA DTPNDALTAR NNGAQGIGLC RTEHMFFASD ERIKAVRKMI
MAVTPEQRKV ALDLLLPYQR SDFEGIFRAM DGLPVTIRLL DPPLHEFLPE GDLEHIVNEL
AVDTGMSADE IYSKIENLSE VNPMLGFRGC RLGISYPELT EMQVRAIFQA AVSMTNQGVT
VIPEIMVPLV GTPQELRHQI SVIRGVAANV FAEMGVTLEY KVGTMIEIPR AALIAEEIGK
EADFFSFGTN DLTQMTFGYS RDDVGKFLQI YLAQGILQHD PFEVIDQKGV GQLIKMATEK
GRAANPNLKV GICGEHGGEP SSVAFFDGVG LDYVSCSPFR VPIARLAAAQ VIV


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