IPR037446
Histidine acid phosphatase, VIP1 family
InterPro entry
Short name | His_Pase_VIP1 |
Overlapping homologous superfamilies | |
family relationships |
Description
This entry represents the VIP1 subfamily of the histidine acid phosphatase family. Budding yeast Vip1 is a inositol hexakisphosphate and inositol heptakisphosphate kinase
[2]. The N-terminal domain of yeast Vip1 has inositol-hexakisphosphate kinase activity and is followed by a phosphatase domain of as yet unknown specificity, but which is very likely to act on multiply phosphorylated inositol species
[1].
The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The relationship between the two branches is not evident by (PSI-)BLAST but is clear from more sensitive sequence searches and structural comparisons
[1].
References
1.The histidine phosphatase superfamily: structure and function. Rigden DJ. Biochem. J. 409, 333-48, (2008). View articlePMID: 18092946
2.Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases. Fridy PC, Otto JC, Dollins DE, York JD. J. Biol. Chem. 282, 30754-62, (2007). View articlePMID: 17690096
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- PANTHER:PTHR12750
Representative structure
8e1j: Asp1 kinase in complex with 1,5-IP8