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Information on EC 2.7.1.159 - inositol-1,3,4-trisphosphate 5/6-kinase and Organism(s) Entamoeba histolytica and UniProt Accession Q9XYQ1

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EC Tree
IUBMB 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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Entamoeba histolytica
UNIPROT: Q9XYQ1
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The taxonomic range for the selected organisms is: Entamoeba histolytica
The enzyme appears in selected viruses and cellular organisms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ins(1,3,4)P3 5/6-kinase
-
additional information
the enzyme belongs to the ATP-grasp family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol-1,3,4-trisphosphate = ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
show the reaction diagram
determination of substrate binding sites, catalytic reaction mechanism
ATP + 1D-myo-inositol-1,3,4-trisphosphate = ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
show the reaction diagram
determination of substrate binding sites, catalytic reaction mechanism
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
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 hide
288307-53-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
show the reaction diagram
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
enzyme expression is slightly induced by heat shock
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ITPK1_ENTHI
319
0
36480
Swiss-Prot
other Location (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme free or in complex with ATP analogue AMP-PCP and substrate inositol-1,3,4-trisphosphate in presence of Mg2+, 30 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 10 mM DTT, mixed with a solution containing 20% PEG 3000, 0.1 M Tris-HCl, pH 7.5, and 0.1 M Ca(OAc)2, several months, crystals are seeded into sitting drops of 15 mg/ml protein, 25% PEG 3350, 5% PEG 400, 0.1 M Bis-Tris, pH 5.5, 10 mM DTT, and 10 mM L-cysteine, with or without ligands added as 10 mM AMP-PCP, 10 mM MgCl2, and 5 mM inositol-1,3,4-trisphosphate, direct X-ray diffraction analysis after this step or further seeding adding ADP and other ligands, overview, X-ray diffraction structure determination and analysis at 1.2-2.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of diverse mutants and analysis of the function of the residues in catalysis and substrate binding, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography and gel filtration
recombinant GST-tagged enzyme, the GST-tag is cleaved off by treatment with GST-3Cpro
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression as GST-tagged enzyme in bacteria
expression of GST-tagged wild-type enzyme and of mutant enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Field, J.; Wilson, M.P.; Mai, Z.; Majerus, P.W.; Samuelson, J.
An Entamoeba histolytica inositol 1,3,4-trisphosphate 5/6-kinase has a novel 3-kinase activity
Mol. Biochem. Parasitol.
108
119-123
2000
Entamoeba histolytica (Q9XYQ1), Entamoeba histolytica HM-1 (Q9XYQ1)
Manually annotated by BRENDA team
Miller, G.J.; Wilson, M.P.; Majerus, P.W.; Hurley, J.H.
Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase
Mol. Cell
18
201-212
2005
Entamoeba histolytica (Q9XYQ1)
Manually annotated by BRENDA team