Protein Family Models

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 larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members. [1]. 18092946. The histidine phosphatase superfamily: structure and function. Rigden DJ;. Biochem J. 2008;409:333-348. (from Pfam)

Date:

2024-10-16

This BlastRule describes Ais (aluminum-induced protein), as found in Escherichia coli. It is nearly 70 percent identical to the lipopolysaccharide core heptose(II)-phosphate phosphatase PmrG of Salmonella (see NBR007184), to which it may be functionally equivalent.

Gene:

ais

Date:

2021-07-22

histidine phosphatase family protein similar to Salmonella lipopolysaccharide core heptose(II)-phosphate phosphatase, which helps remodel lipopolysaccharide via removal of the Hep(II) phosphate in the LPS inner core region

Date:

2017-07-31

Catalyzes the of heptose(II) of the outer membrane lipopolysaccharide core

Date:

2020-10-26