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Information on EC 2.7.1.159 - inositol-1,3,4-trisphosphate 5/6-kinase and Organism(s) Arabidopsis thaliana and UniProt Accession O81893
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EC Tree
2.7.1.159 inositol-1,3,4-trisphosphate 5/6-kinaseIUBMB Comments
In humans, this enzyme, along with EC 2.7.1.127 (inositol-trisphosphate 3-kinase), EC 2.7.1.140 (inositol-tetrakisphosphate 5-kinase) and EC 2.7.1.158 (inositol pentakisphosphate 2-kinase) is involved in the production of inositol hexakisphosphate (InsP6). InsP6 is involved in many cellular processes, including mRNA export from the nucleus . Yeasts do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3 by the actions of EC 2.7.1.151 (inositol-polyphosphate multikinase) and EC 2.7.1.158 (inositol-pentakisphosphate 2-kinase) . The enzymes from animals and plants also have the activity of EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase.
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Word Map
- 2.7.1.159
-
phytic
- polyphosphate
-
hexakisphosphate
- dehydration
-
itpks
-
2-kinase
- phosphorus
- pentakisphosphate
-
signalosome
-
lipid-independent
-
tnfalpha-induced
- 1,3,4,5,6-pentakisphosphate
-
monophosphatase
-
photomorphogenesis
-
1,4,5-tris-phosphate
- 1,3,4,6-tetrakisphosphate
- phytate
- imp
- ikappabalpha
-
atp-grasp
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(3 overall reactions are displayed. Show all (4)>>)
Synonyms
5/6-kinase, gmitpk2, ositl1, 5/6 kinase, atitpk4, inositol 1,3,4-triphosphate 5/6-kinase, at2g43980, inositol-1,3,4-trisphosphate 5/6-kinase, inositol-1,3,4-trisphosphate kinase, ins(1,3,4)p3 5/6-kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
inositol 1,3,4-trisphosphate 5/6-kinase
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol 1,3,4-trisphosphate 5-phosphotransferase
In humans, this enzyme, along with EC 2.7.1.127 (inositol-trisphosphate 3-kinase), EC 2.7.1.140 (inositol-tetrakisphosphate 5-kinase) and EC 2.7.1.158 (inositol pentakisphosphate 2-kinase) is involved in the production of inositol hexakisphosphate (InsP6). InsP6 is involved in many cellular processes, including mRNA export from the nucleus [2]. Yeasts do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3 by the actions of EC 2.7.1.151 (inositol-polyphosphate multikinase) and EC 2.7.1.158 (inositol-pentakisphosphate 2-kinase) [2]. The enzymes from animals and plants also have the activity of EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase.
CAS REGISTRY NUMBER
COMMENTARY
288307-53-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,6-trisphosphate + 1D-myo-inositol 3,4,6-trisphosphate
ADP + inositol tetrakisphosphate
racemic mix of phosphates
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
-
-
?
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
-
-
-
?
1D-myo-inositol-1,4,5,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
AtITPK4 is more active against 1D-myo-inositol-1,4,5,6-tetrakisphosphate than against 1D-myo-inositol-3,4,5,6-tetrakisphosphate.
-
-
?
1D-myo-inositol-1,4,6-trisphosphate + 1D-myo-inositol-3,4,6-trisphosphate + 2 ATP
2 1D-myo-inositol-1,3,4,6-tetrakisphosphate + 2 ADP
racemic mixture
-
-
?
1D-myo-inositol-3,4,5,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
-
-
?
ATP + 1D-myo-inositol 1,4,6-trisphosphate + 1D-myo-inositol 3,4,6-trisphosphate
ADP + inositol tetrakisphosphate
racemic mix of phosphates
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
?
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
recombinant enzyme, 3fold lower activity compared to 1D-myo-inositol-1,3,4,6-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
recombinant enzyme, 3fold higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
The substrate is converted to InsP4 but not to InsP5
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
additional information
?
-
the enzyme also performs the reaction of EC 2.7.1.134, phosphorylation of position 1 of 1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
-
?
additional information
?
-
the enzyme is involved in photomorphogenesis under red light conditions
-
-
?
additional information
?
-
the enzyme performs autophosphorylation, the enzyme is associated with the COP9 signalosome, i.e. CSN
-
-
?
additional information
?
-
the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
-
-
?
additional information
?
-
the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
-
-
?
additional information
?
-
the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
-
-
?
additional information
?
-
the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
-
-
?
additional information
?
-
-
the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
the enzyme also performs the reaction of EC 2.7.1.134, phosphorylation of position 1 of 1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,6-trisphosphate + 1D-myo-inositol 3,4,6-trisphosphate
ADP + inositol tetrakisphosphate
racemic mix of phosphates
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
-
-
?
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
-
-
-
?
1D-myo-inositol-1,4,6-trisphosphate + 1D-myo-inositol-3,4,6-trisphosphate + 2 ATP
2 1D-myo-inositol-1,3,4,6-tetrakisphosphate + 2 ADP
racemic mixture
-
-
?
1D-myo-inositol-3,4,5,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
-
-
?
ATP + 1D-myo-inositol 1,4,6-trisphosphate + 1D-myo-inositol 3,4,6-trisphosphate
ADP + inositol tetrakisphosphate
racemic mix of phosphates
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
The substrate is converted to InsP4 but not to InsP5
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
additional information
?
-
the enzyme is involved in photomorphogenesis under red light conditions
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
-
enzyme displays both kinase and phosphatase activity.
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
-
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme belongs to a larger family of ATP-grasp fold proteins
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
young, AtITPK4 transcript is expressed throughout early flower development which culminates in the opening of the flower bud
additional information
expressed in male and female organs of young and mature flowers
weak expression, revealed expression in the seed and pod wall
additional information
expression pattern of isozyme ITPK2, no or very poor expression in stem
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the epidermis structure of seed coat is irregularly formed in seeds of itpk2-1 mutant, resulting in the increased permeability of seed coat to tetrazolium salts. The cell wall shows a dramatic decrease in composition of suberin and cutin, which relate to the permeability of seed coat and the formation of which is accompanied with seed coat development. ITPK2 deficiency results in the distorted seed coat and crumpled columellas. Seed coat of itpk2-1 mutant presents high permeability to 2,3,5-triphenyltetrazolium and has less mucilage
physiological function
enzyme ITPK2 plays an essential role in seed coat development and lipid polyester barrier formation
malfunction
metabolism
physiological function
the enzyme is required for phytate (inositol hexakisphosphate, InsP6) synthesis and involved in maintaining phosphate homeostasis under phosphate-replete conditions
malfunction
loss of this gene in itpk3-1 does neither affect phytate seed levels, nor seed Zn, Fe, and Mn but the micronutrient bioavailability is strongly reduced by seed phytate that forms complexes with seed cations. Low seed zinc is primarily caused by plant growth in Zn-deficient soil
malfunction
although both ipk1-1 and itpk1 mutants exhibit decreased levels of InsP6 (phytate) and diphosphoinositol pentakisphosphate (PP-InsP5, InsP7), disruption of another ITPK family enzyme, ITPK4, which correspondingly causes depletion of InsP6 and InsP7, does not display similar phosphate-related phenotypes, which precludes these InsP species from being effectors. Notably, the level of D/L-Ins(3,4,5,6)P4 is concurrently elevated in both ipk1-1 and itpk1 mutants, which demonstrates a specific correlation with the misregulated phosphate phenotypes. The level of D/L-Ins(3,4,5,6)P4 is not responsive to phosphate starvation that instead manifests a shoot-specific increase in the InsP7 level. ITPK1 overexpression significantly decreases phosphate uptake activity, in contrast to the elevated uptake activity shown by itpk1 mutants. In addition, several PSR genes are downregulated in ITPK1-overexpressing lines compared with the wild-type (e.g. PHT1:2, SPX1, AT4, IPS1 and PAP17)
metabolism
measurement of Fe, Zn, and Mn concentrations in seeds of Arabidopsis thaliana accessions grown in Zn-deficient and Zn-amended conditions, overview. Inositol 1,3,4-trisphosphate 5/6-kinase 3 gene (ITPK3), located close to a significant nucleotide polymorphism associated with relative Zn seed concentrations, is dispensable for seed micronutrients accumulation in ecotype Col-0
metabolism
the kinase activity of inositol pentakisphosphate 2-kinase (IPK1) is required for phytate (inositol hexakisphosphate, InsP6) synthesis, and is indispensable for maintaining phosphate homeostasis under phosphate-replete conditions. Inositol 1,3,4-trisphosphate 5/6-kinase 1 (ITPK1) plays an equivalent role. Genetic dissection of the roles for InsP and PP-InsP biosynthesis enzymes in regulation of phosphate homeostasis, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ITPK2_ARATH
391
0
44172
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
functional analysis of itpk2-1 mutant (SAIL_25_H09), phenotype, overview
additional information
construction of an enzyme-deficient mutant line, phenotype with reduced hypocotyl
additional information
construction of the homogenous At4g08170 mutant (SALK_120653C, NASCcode N653925) carrying a T-DNA insertion in the intron in wild-type line Col-0
additional information
generation of itpk1-1 mutants, phenotype, overview. Genetic interaction analysis of bifunctional ITPK1 (EC 2.7.1.159/EC 2.7.1.134) and IPK1 (EC 2.7.1.158) with a genetic cross between ipk1-1 and itpk1 mutants. The ipk1-1 itpk1 double mutants exhibit more severe growth defects than single mutants and those that proceeded to the reproductive stage bore aborted seeds. Common elevation of D/L-Ins(3,4,5,6)P4 in itpk1 and ipk1-1 mutants
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS/PAGE. Protein concentration is determined by the Bradford method.
Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS-PAGE. Protein concentration is determined by the Bradford assay.
Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS-PAGE. Protein concentration is determined by the Bradford method.
Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS/PAGE. Protein concentration is determined by Bradford assay.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ITPK2, expression analysis of wild-type and mutant enzymes by quantitative real-time PCR analysis
in Escherichia coli Rosetta, transformed with pET28a and pET28c containing 3 kinase cDNAs. Vector-encoded hexa-histidine (His) tags are added to all proteins.
DNA and amino acid sequence determination and analysis, expression as tagged enzyme in Escherichia coli
-
gene itpk3-1, genotyping, 108 different accessions, the Arabidopsis accessions differ in their response to Zn deficiency, quantitative real-time PCR enzyme expression anaysis, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilson, M.P.; Majerus, P.W.
Characterization of a cDNA encoding Arabidopsis thaliana inositol 1,3,4-trisphosphate 5/6-kinase
Biochem. Biophys. Res. Commun.
232
678-681
1997
Arabidopsis thaliana
Qin, Z.X.; Chen, Q.J.; Tong, Z.; Wang, X.C.
The Arabidopsis inositol 1,3,4-trisphosphate 5/6 kinase, AtItpk-1, is involved in plant photomorphogenesis under red light conditions, possibly via interaction with COP9 signalosome
Plant Physiol. Biochem.
43
947-954
2005
Arabidopsis thaliana (Q9SUG3)
Sweetman, D.; Stavridou, I.; Johnson, S.; Green, P.; Caddick, S.E.; Brearley, C.A.
Arabidopsis thaliana inositol 1,3,4-trisphosphate 5/6-kinase 4 (AtITPK4) is an outlier to a family of ATP-grasp fold proteins from Arabidopsis
FEBS Lett.
581
4165-4171
2007
Arabidopsis thaliana (O80568), Arabidopsis thaliana (O81893), Arabidopsis thaliana (Q9SBA5), Arabidopsis thaliana (Q9SUG3), Arabidopsis thaliana
Tang, Y.; Tan, S.; Xue, H.
Arabidopsis inositol 1,3,4-trisphosphate 5/6 kinase 2 is required for seed coat development
Acta Biochim. Biophys. Sin. (Shanghai)
45
549-560
2013
Arabidopsis thaliana (O81893)
Chen, X.; Yuan, L.; Ludewig, U.
Natural genetic variation of seed micronutrients of Arabidopsis thaliana grown in zinc-deficient and zinc-amended soil
Front. Plant Sci.
7
1070
2016
Arabidopsis thaliana (Q9SUG3), Arabidopsis thaliana Col-0 (Q9SUG3)
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