The former function (EC220.127.116.11), found at the N-terminal, dehydrated d-erythroimidazoleglycerolphosphate to imidazoleacetolphosphate, the latter function (EC18.104.22.168), found at the C-terminal, dephosphorylates l-histidinolphosphate producing histidinol.
The firth step is catalysed instead by histadinolphosphate aminotransferase (encoded by hisC)
The peptide is 40.5kDa and associates to form a hexamer (unless truncated)
In E. coli hisB is found on the hisGDCBHAFI operon
The phosphatase activity possess a substrate ambiguity and overexpression of hisB can rescue phosphoserine phosphatase (serB) knockouts.
HIS3 from Saccharomyces cerevisiae is not a fused IGP dehydratase and hisidinol phosphatase, but an IGPD only (homologous to hisB-N). Whereas HIS2 is the HP (analogous to hisB-C, called hisJ in some prokaryotes).
^Parker95: Parker, A.R., Moore, J.A., Schwab, J.M., Davisson, V.J. (1995). "Escherichia coli Imidazoleglycerol Phosphate Dehydratase: Spectroscopic Characterization of the Enzymic Product and the Steric Course of the Reaction." Journal of the American Chemical Society.