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Information on EC 2.7.11.32 - [pyruvate, phosphate dikinase] kinase and Organism(s) Arabidopsis thaliana and UniProt Accession O23404

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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This record set is specific for:
Arabidopsis thaliana
UNIPROT: O23404
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
[pyruvate, phosphate dikinase]
=
+
[pyruvate, phosphate dikinase] phosphate
Synonyms
ADP:protein phosphotransferase, AtRP1, AtRP2, bifunctional regulatory protein, PDRP, PPDK regulatory protein, PPDK regulatory protein 1, PPDK regulatory protein 2, pyruvate, orthophosphate dikinase regulatory protein, pyruvate, orthophosphate dikinase regulatory protein 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AtRP1
298911
-
AtRP2
298912
-
PPDK regulatory protein 1
298913
-
PPDK regulatory protein 2
302
-
pyruvate, orthophosphate dikinase regulatory protein 1
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
active
inactive
-
?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.7.9.1
UniProt
Manually annotated by BRENDA team
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
PPDK1_ARATH
963
0
105138
Swiss-Prot
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
His-tagged protein expressed in Escherichia coli BL21(DE3)pLysS
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, Arabidopsis thaliana (O49562), Arabidopsis thaliana (Q9MAC9)
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
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