Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.150
Description:1-phosphatidylinositol-3-phosphate 5-kinase.
Alternative Name: Type III PIP kinase.
Phosphatidylinositol 3-phosphate 5-kinase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.150
BRENDA Enzyme Link: BRENDA 2.7.1.150
KEGG Enzyme Link: KEGG2.7.1.150
BioCyc Enzyme Link: BioCyc 2.7.1.150
ExPASy Enzyme Link: ExPASy2.7.1.150
EC2PDB Enzyme Link: EC2PDB 2.7.1.150
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.150
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.150
IntEnz Enzyme Link: IntEnz 2.7.1.150
MEDLINE Enzyme Link: MEDLINE 2.7.1.150
MSA:

2.7.1.150;

Phylogenetic Tree:

2.7.1.150;

Uniprot:
M-CSA:
RHEA:13609 a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 3-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + ADP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:1]-[O;H0;+0:2]-[P;H0;+0:4](=[*:3])(-[*:5])-[*:6].[*:8]-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae.Cooke FT, Dove SK, McEwen RK, Painter G, Holmes AB, Hall MN, Michell RH, Parker PJ1998 Nov 59811604
Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases.McEwen RK, Dove SK, Cooke FT, Painter GF, Holmes AB, Shisheva A, Ohya Y, Parker PJ, Michell RH1999 Nov 2610567352