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MetaCyc Enzyme: phosphatidylinositol 5-phosphatase

Gene: 5PTase11 Accession Number: AT1G47510 (MetaCyc)

Species: Arabidopsis thaliana col

Summary:
5PTase11 has phosphatidylinositol polyphosphate 5-phosphatase activity against a 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate, and 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate when its activity is tested in vitro following expression in insect cells [Ercetin04]. Meanwhile, under the same experimental conditions, no activity is observed with the monophosphorylated phosphotidyl inositol PI(5)P nor with the soluble D-myo-inositol (1,4,5)-trisphosphate or D-myo-inositol (1,3,4,5)-tetrakisphosphate [Ercetin04].

This protein is the smallest of the putative 15 members of the inositol polyphosphate 5-phosphatase family in Arabidopsis [Ercetin04].

5PTase11 transcripts appear to be expressed throughout the plant but seem to be present at higher levels in roots than in other organs. In addition, 5PTase11 transcript expression levels appear to increase in response to a treatment with auxin and jasmonic acid [Ercetin04].

Map Position: [17,438,041 -> 17,440,836]

Unification Links: Phytozome Plant Orthologs:AT1G47510.1 , TAIR:AT1G47510 , UniProt:Q5EAF2

Gene-Reaction Schematic: ?

Gene Class: UNCLASSIFIED

Credits:
Imported from AraCyc 16-Apr-2012 by Dreher KA , PMN


Enzymatic reaction of: PI(3,5)P25'phosphatase (phosphatidylinositol 5-phosphatase)

EC Number: 3.1.3.-

1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O <=> a 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: PI(3,4,5)P3 5-phosphatase (phosphatidylinositol 5-phosphatase)

EC Number: 3.1.3.86

1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O <=> a 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Summary:
The Vmax with 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate is 235 pmol/µg/min [Zhong04].

As of 2010, PI(3,4,5)P3 had not been identified in plants so it is unclear whether this in vitro activity has any biological relevance [Zhao10c].

Activators (Unknown Mechanism): Mg2+ [Zhong04]


Enzymatic reaction of: phosphatidylinositol-4,5-bisphosphate 5-phosphatase (phosphatidylinositol 5-phosphatase)

EC Number: 3.1.3.36

a 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O <=> a 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from AraCyc 16-Apr-2012 by Dreher KA , PMN


References

Chi09: Chi A, Rhee S (2009). "The functional annotation of Arabidopsis protein sequences was performed by BLAST queries against a reference set of experimentally verified enzymes. For each Arabidopsis sequence, the enzymatic activity of the top BLAST hit (or hits if they had equivalent E-values) was assigned to the protein if its E-value fell below a specific E-value threshold established for the corresponding enzymatic activity. Note: The annotation thresholds were established by doing a self BLAST of the reference enzyme dataset. For each enzymatic activity represented by multiple proteins, the mean E-value of all the correct hits generated by the self BLAST was selected as the cut-off. All of these means were averaged and used as the cut-off for assigning annotations for any enzymatic activities that were represented by a single protein in the reference dataset."

Ercetin04: Ercetin ME, Gillaspy GE (2004). "Molecular characterization of an Arabidopsis gene encoding a phospholipid-specific inositol polyphosphate 5-phosphatase." Plant Physiol 135(2);938-46. PMID: 15181205

Lecompte08: Lecompte O, Poch O, Laporte J (2008). "PtdIns5P regulation through evolution: roles in membrane trafficking?." Trends Biochem Sci 33(10);453-60. PMID: 18774718

Rohde02: Rohde G, Wenzel D, Haucke V (2002). "A phosphatidylinositol (4,5)-bisphosphate binding site within mu2-adaptin regulates clathrin-mediated endocytosis." J Cell Biol 158(2);209-14. PMID: 12119359

Zhang07c: Zhang Y, Zolov SN, Chow CY, Slutsky SG, Richardson SC, Piper RC, Yang B, Nau JJ, Westrick RJ, Morrison SJ, Meisler MH, Weisman LS (2007). "Loss of Vac14, a regulator of the signaling lipid phosphatidylinositol 3,5-bisphosphate, results in neurodegeneration in mice." Proc Natl Acad Sci U S A 104(44);17518-23. PMID: 17956977

Zhao10c: Zhao Y, Yan A, Feijo JA, Furutani M, Takenawa T, Hwang I, Fu Y, Yang Z (2010). "Phosphoinositides regulate clathrin-dependent endocytosis at the tip of pollen tubes in Arabidopsis and tobacco." Plant Cell 22(12);4031-44. PMID: 21189293

Zhong04: Zhong R, Ye ZH (2004). "Molecular and biochemical characterization of three WD-repeat-domain-containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana." Plant Cell Physiol 45(11);1720-8. PMID: 15574849


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, BIOCYC13A.