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Information on EC 2.7.11.32 - [pyruvate, phosphate dikinase] kinase and Organism(s) Arabidopsis thaliana and UniProt Accession O49562

for references in articles please use BRENDA:EC2.7.11.32
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EC Tree
IUBMB Comments
The enzymes from the plants Zea mays (maize) and Arabidopsis thaliana are bifunctional and catalyse both the phosphorylation and dephosphorylation of EC 2.7.9.1 (pyruvate, phosphate dikinase). cf. EC 2.7.4.27, [pyruvate, phosphate dikinase]-phosphate phosphotransferase [2-5]. The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates a threonine located adjacent to the catalytic histidine. The phosphorylation only takes place if the histidine is already phosphorylated [3-5].
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Arabidopsis thaliana
UNIPROT: O49562
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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ADP
+
[pyruvate, phosphate dikinase]
=
AMP
+
[pyruvate, phosphate dikinase] phosphate
+
[pyruvate, phosphate dikinase]
=
+
[pyruvate, phosphate dikinase] phosphate
Synonyms
regulatory protein, bifunctional regulatory protein, atrp2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyruvate, orthophosphate dikinase regulatory protein 1
bifunctional Ser/Thr protein kinase/protein phosphatase
PPDK regulatory protein 1
-
PPDK regulatory protein 2
-
-
pyruvate, orthophosphate dikinase regulatory protein 1
bifunctional
pyruvate, orthophosphate dikinase regulatory protein 2
SYSTEMATIC NAME
IUBMB Comments
ADP:[pyruvate, phosphate dikinase] phosphotransferase
The enzymes from the plants Zea mays (maize) and Arabidopsis thaliana are bifunctional and catalyse both the phosphorylation and dephosphorylation of EC 2.7.9.1 (pyruvate, phosphate dikinase). cf. EC 2.7.4.27, [pyruvate, phosphate dikinase]-phosphate phosphotransferase [2-5]. The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates a threonine located adjacent to the catalytic histidine. The phosphorylation only takes place if the histidine is already phosphorylated [3-5].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
show the reaction diagram
His458 phosphorylated (active), maize wild type and T456S mutant pyruvate, phosphate dikinase serve as substrate, T456V mutant pyruvate, phosphate dikinase serves not as substrate
His458 and Thr456 phosphorylated (inactive)
-
?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PDRP1_ARATH
403
0
43684
Swiss-Prot
Chloroplast (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
immobilized metal ion affinity chromatography (Ni2+)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3)
His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3)
His-tagged protein expressed in Escherichia coli BL21(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chastain, C.J.; Xu, W.; Parsley, K.; Sarath, G.; Hibberd, J.M.; Chollet, R.
The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure
Plant J.
53
854-863
2008
Arabidopsis thaliana (O49562), Arabidopsis thaliana (Q9MAC9), Arabidopsis thaliana
Manually annotated by BRENDA team
Astley, H.; Parsley, K.; Aubry, S.; Chastain, C.; Burnell, J.; Webb, M.; Hibberd, J.
The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis are both bifunctional and interact with the catalytic and nucleotide-binding domains of pyruvate, orthophosphate dikinase
Plant J.
68
1070-1080
2011
Arabidopsis thaliana, Arabidopsis thaliana (O23404)
Manually annotated by BRENDA team