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Information on EC 2.7.1.68 - 1-phosphatidylinositol-4-phosphate 5-kinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8L850
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2.7.1.68 1-phosphatidylinositol-4-phosphate 5-kinaseIUBMB Comments
This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known.
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Word Map
- 2.7.1.68
- 4,5-bisphosphate
- phosphoinositide
- fracture
- pip2
- actin
- femoral
- phospholipase
-
ptdins4,5p2
- phospholipid
- cytoskeleton
- dislocation
- phosphatidylinositol-4,5-bisphosphate
-
phosphatidic
-
posterior
- gtpases
- diacylglycerol
-
4-kinase
-
polyphosphoinositides
-
acetabular
-
accident
-
ossification
- talin
-
avascular
- rac1
-
fracture-dislocation
- bisphosphate
-
screw
- arf6
-
5-phosphatase
-
heterotopic
-
arthroplasty
- 3,4,5-trisphosphate
-
ptdins5p
-
trochanteric
-
ovcar-5
- osteonecrosis
-
inositide
-
osteotomy
-
kinase-dead
-
osteochondral
- tiazofurin
-
3hinositol
-
insps
-
merle
-
ptdins3,4,5p3
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
pipkin, pip5k, pip kinase, ptdinsp, phosphatidylinositol 4-phosphate 5-kinase, phosphatidylinositol-4-phosphate 5-kinase, pipk, pipkigamma, pip5k1a, pip5ks, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Diphosphoinositide kinase
-
-
-
-
MSS4p
-
-
-
-
phosphatidylinositol 4-phosphate 5-kinase
phosphatidylinositol 4-phosphate kinase
-
-
-
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phosphatidylinositol phosphate 5-kinase
phosphatidylinositol-4-phosphate 5-kinase
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-
-
-
PI4P 5-kinase
PI4P5K
-
-
-
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PIP kinase
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-
-
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PIP-5kin
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-
-
-
PIP5K
PIP5K2
PIP5K3
PIP5K3 encodes the enzyme activity producing PtdIns(4,5)P2.
PIP5Ks
-
-
-
-
PtdIns(4)P 5-kinase
-
-
-
-
additional information
PI4P 5-kinase
-
-
-
-
PIP5K
-
-
-
-
PIP5K
Arabidopsis genome contains 11 genes encoding proteins with significant sequence similarity to animal PIP5Ks. These are classified into two subfamilies: subfamily A proteins (PIP5K10 and PIP5K11) consist of dimerization and catalytic domains similar to those in the animal enzymes, while subfamily B proteins (PIP5K1 to PIP5K9) have an additional domain containing a repeat of the membrane occupation and recognition nexus motif at the N-terminus.
additional information
phosphatidylinositol phosphate 5-kinase 1 belongs to the subfamily B
additional information
phosphatidylinositol phosphate 5-kinase 10 belongs to the subfamily A
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase
This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known.
CAS REGISTRY NUMBER
COMMENTARY
104645-76-3
-
9032-61-5
-
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 + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
-
PIP5K3 is involved in localizing 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate to the elongating root hair apex and is a key regulator of the machinery that initiates and promotes root hair tip growth.
-
r
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
enzyme is induced by water stress and abscisic acid. The enzyme is involved in water-stress signal transduction
-
-
?
additional information
?
-
GST-PIP5K3 produces 1-phosphatidyl-1D-myo-inositol 4,5 by phosphorylating 1-phosphatidyl-1D-myo-inositol 4-phosphate, both the natural and synthetic forms. Its also phosphorylates 1-phosphatidyl-1D-myo-inositol 5-phosphate, but less efficiently. PIP5K3 catalyzes the synthesis of 1-phosphatidyl-1D-myo-inositol 4,5 preferentially from 1-phosphatidyl-1D-myo-inositol 4-phosphate in vitro.
-
-
?
additional information
?
-
-
GST-PIP5K3 produces 1-phosphatidyl-1D-myo-inositol 4,5 by phosphorylating 1-phosphatidyl-1D-myo-inositol 4-phosphate, both the natural and synthetic forms. Its also phosphorylates 1-phosphatidyl-1D-myo-inositol 5-phosphate, but less efficiently. PIP5K3 catalyzes the synthesis of 1-phosphatidyl-1D-myo-inositol 4,5 preferentially from 1-phosphatidyl-1D-myo-inositol 4-phosphate in vitro.
-
-
?
additional information
?
-
PIP5K3 may function as a downstream effector of rho-related GTPases of plants (ROPs) in regulatory mechanisms, not only for the planar polarity of bulge initiation but also for the promotion of root hair tip growth.
-
-
?
additional information
?
-
-
PIP5K3 may function as a downstream effector of rho-related GTPases of plants (ROPs) in regulatory mechanisms, not only for the planar polarity of bulge initiation but also for the promotion of root hair tip growth.
-
-
?
additional information
?
-
Reduced expression of functional PIP5K3 is responsible for the short-root hair phenotype. Inducible overexpression of PIP5K3 enhanced root hair elongation and increased the rate of 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
-
-
?
additional information
?
-
-
Reduced expression of functional PIP5K3 is responsible for the short-root hair phenotype. Inducible overexpression of PIP5K3 enhanced root hair elongation and increased the rate of 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
-
-
?
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 + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
-
PIP5K3 is involved in localizing 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate to the elongating root hair apex and is a key regulator of the machinery that initiates and promotes root hair tip growth.
-
r
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
enzyme is induced by water stress and abscisic acid. The enzyme is involved in water-stress signal transduction
-
-
?
additional information
?
-
GST-PIP5K3 produces 1-phosphatidyl-1D-myo-inositol 4,5 by phosphorylating 1-phosphatidyl-1D-myo-inositol 4-phosphate, both the natural and synthetic forms. Its also phosphorylates 1-phosphatidyl-1D-myo-inositol 5-phosphate, but less efficiently. PIP5K3 catalyzes the synthesis of 1-phosphatidyl-1D-myo-inositol 4,5 preferentially from 1-phosphatidyl-1D-myo-inositol 4-phosphate in vitro.
-
-
?
additional information
?
-
-
GST-PIP5K3 produces 1-phosphatidyl-1D-myo-inositol 4,5 by phosphorylating 1-phosphatidyl-1D-myo-inositol 4-phosphate, both the natural and synthetic forms. Its also phosphorylates 1-phosphatidyl-1D-myo-inositol 5-phosphate, but less efficiently. PIP5K3 catalyzes the synthesis of 1-phosphatidyl-1D-myo-inositol 4,5 preferentially from 1-phosphatidyl-1D-myo-inositol 4-phosphate in vitro.
-
-
?
additional information
?
-
PIP5K3 may function as a downstream effector of rho-related GTPases of plants (ROPs) in regulatory mechanisms, not only for the planar polarity of bulge initiation but also for the promotion of root hair tip growth.
-
-
?
additional information
?
-
-
PIP5K3 may function as a downstream effector of rho-related GTPases of plants (ROPs) in regulatory mechanisms, not only for the planar polarity of bulge initiation but also for the promotion of root hair tip growth.
-
-
?
additional information
?
-
Reduced expression of functional PIP5K3 is responsible for the short-root hair phenotype. Inducible overexpression of PIP5K3 enhanced root hair elongation and increased the rate of 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
-
-
?
additional information
?
-
-
Reduced expression of functional PIP5K3 is responsible for the short-root hair phenotype. Inducible overexpression of PIP5K3 enhanced root hair elongation and increased the rate of 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme form 10 is insensitive to phosphatidic acid
-
additional information
enzyme form 10 is insensitive to phosphatidic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.065
1-phosphatidyl-1D-myo-inositol 4-phosphate
recombinant enzyme form 10
0.6
1-phosphatidyl-1D-myo-inositol 4-phosphate
recombinant enzyme form 1
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme form 10 shows 10fold lower activity than enzyme form 1 in recombinant Sf9 cells, overview
additional information
enzyme form 10 shows 10fold lower activity than enzyme form 1 in recombinant Sf9 cells, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Escherichia coli BL21 cell is used for cloning and expression
additional information
t-DNA insertion mutations that reduces the expression of PIP5K3 cause shorter root hairs than in the wild type. Overexpression causes longer root hairs and multiple protruding sites on a single trichoblast.
-
enzyme localizes to the periphery of the apical region of root hair cells
additional information
tissue distribution, enzyme form 1 is present in all tissues
additional information
tissue distribution, enzyme form 1 is present in all tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
cytoplasmic space of elongating root hair apices
-
additional information
-
cytoplasmic space of elongating root hair apices
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
isoform PIP5K2 interacts physically with alpha-importin isoforms IMPalpha6 and IMPalpha9
physiological function
malfunction
-
enzyme mutants exhibit shorter root hairs than the wild type and remained responsive to phosphate deficiency in root hair elongation
malfunction
-
the loss of function of isoforms PIP5K1 and PIP5K2 produces defects on vacuoles and exine wall in pollen grains
physiological function
-
isoform PIP5K3 and PIP5K4 are redundantly required for the root hair elongation response at young seedling stages
physiological function
-
phosphatidylinositol 4-phosphate 5-kinases 1 and 2 are involved in the regulation of vacuole morphology during Arabidopsis thaliana pollen development. Both isoforms are involved in protein trafficking to the vacuole in root tip epidermal cells
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). PI5K9_ARATH
815
0
92092
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
T-DNA insertion mutant pip5k9-d shows enhanced PIP5K9 transcript levels
additional information
-
T-DNA insertion mutant pip5k9-d shows enhanced PIP5K9 transcript levels
additional information
-
mutant plants homozygous for T-DNA-disrupted PIP5K3 alleles are compromised in root hair formation. Root hair-specific PIP5K3 overexpression results in root hair deformation and loss of cell polarity with increasing accumulation of PIP5K3 transcript. An N-terminal domain containing membrane occupation and recognition nexus repeats, which is not required for catalytic activity, is essential for the establishment of root hair growth. Transient heterologous expression of full-length PIP5K3 in Nicotiana tabacum pollen tubes increases plasma membrane association of a phosphatidylinositol 4,5-bisphoshate-specific reporter
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Partial purification from Escherichia coli culture cells. The cells are suspended in PBS buffer, sonicated on ice, and centrifuged. Supernatant is mixed with glutathione-Sepharose 4B and incubated at 48°C for 2 h. The Sepharose beads are collected and washed with an excess volume of PBS.
recombinant GST-fusion protein from Escherichia coli in presence of Triton X-100 and PtdOH
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a yellow fluorescent (YFP) und GUS fusion PIP5K3 protein is expressed in Escherichia coli cells and transformed in Arabidopsis thaliana to produce trangenic plants. Overexpression and mutant is investigated.
expressed in Escherichia coli strain Rosetta2 cells and Allium cepa epidermis cells
-
expression of enzyme form 1 as GST-fusion protein in Escherichia coli, expression of His-tagged enzyme form 1 in Spodoptera frugiperda Sf9 cells via baculovirus infection system
expression of enzyme form 10 as GST-fusion protein in Escherichia coli, expression of His-tagged enzyme form 10 in Spodoptera frugiperda Sf9 cells via baculovirus infection system
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme transcript levels increase in response to auxin and indole 3-acetic acid
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mikami, K.; Katagiri, T.; Iuchi, S.; Yamaguchi-Shinozaki, K.; Shinozaki, K.
A gene encoding phosphatidylinositol-4-phosphate 5-kinase is induced by water stress and abscisic acid in Arabidopsis thaliana
Plant J.
15
563-568
1998
Arabidopsis thaliana
Perera, I.Y.; Davis, A.J.; Galanopoulou, D.; Im, Y.J.; Boss, W.F.
Characterization and comparative analysis of Arabidopsis phosphatidylinositol phosphate 5-kinase 10 reveals differences in Arabidopsis and human phosphatidylinositol phosphate kinases
FEBS Lett.
579
3427-3432
2005
Arabidopsis thaliana (Q56YP2), Arabidopsis thaliana (Q9LMN1), Homo sapiens (Q99755), Homo sapiens
Lou, Y.; Gou, J.Y.; Xue, H.W.
PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase, interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth
Plant Cell
19
163-181
2007
Arabidopsis thaliana (Q8L850), Arabidopsis thaliana
Kusano, H.; Testerink, C.; Vermeer, J.E.; Tsuge, T.; Shimada, H.; Oka, A.; Munnik, T.; Aoyama, T.
The arabidopsis phosphatidylinositol phosphate 5-kinase PIP5K3 is a key regulator of root hair tip growth
Plant Cell
20
367-380
2008
Arabidopsis thaliana (O48709), Arabidopsis thaliana
Stenzel, I.; Ischebeck, T.; Koenig, S.; Ho?ubowska, A.; Sporysz, M.; Hause, B.; Heilmann, I.
The type B phosphatidylinositol-4-phosphate 5-kinase 3 is essential for root hair formation in Arabidopsis thaliana
Plant Cell
20
124-141
2008
Arabidopsis thaliana
Wada, Y.; Kusano, H.; Tsuge, T.; Aoyama, T.
Phosphatidylinositol phosphate 5-kinase genes respond to phosphate deficiency for root hair elongation in Arabidopsis thaliana
Plant J.
81
426-437
2015
Arabidopsis thaliana
Ugalde, J.M.; Rodriguez-Furlan, C.; Rycke, R.D.; Norambuena, L.; Friml, J.; Leon, G.; Tejos, R.
Phosphatidylinositol 4-phosphate 5-kinases 1 and 2 are involved in the regulation of vacuole morphology during Arabidopsis thaliana pollen development
Plant Sci.
250
10-19
2016
Arabidopsis thaliana
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