The hisB gene, found in the enterobacteria (such as E. coli), in Campylobacter jejuni and in Xylella/Xanthomonas encodes a protein involved in catalysis of two step in histidine biosynthesis (the sixth and eight step), namely the bifunctional Imidazoleglycerol-phosphate dehydratase/histidinol-phosphatase. The former function, found at the N-terminal, dehydrated d -erythroimidazoleglycerolphosphate to imidazoleacetolphosphate, the latter function , 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.

Reactions

hisB-N hisB-C

Non-fusion protein in other species

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).