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.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.
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 D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O hisB-C L-histidinol phosphate + H2O L-histidinol + phosphate
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).
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