hisB

{{DISPLAYTITLE:hisB}}

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.{{Cite journal

| last1 = Brilli | first1 = M.

| last2 = Fani | first2 = R.

| doi = 10.1007/s00239-003-2547-x

| title = Molecular Evolution of hisB Genes

| journal = Journal of Molecular Evolution

| volume = 58

| issue = 2

| pages = 225–237

| year = 2004

| pmid = 15042344

| bibcode = 2004JMolE..58..225B

| s2cid = 1684458

}}

The former function ({{EC number|4.2.1.19}}), found at the N-terminal, dehydrated d-erythroimidazoleglycerolphosphate to imidazoleacetolphosphate, the latter function ({{EC number|3.1.3.15}}), 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.{{Cite journal

| last1 = Grisolia | first1 = V.

| last2 = Carlomagno | first2 = M. S.

| last3 = Bruni | first3 = C. B.

| title = Cloning and expression of the distal portion of the histidine operon of Escherichia coli K-12

| journal = Journal of Bacteriology

| volume = 151

| issue = 2

| pages = 692–700

| year = 1982

| doi = 10.1128/jb.151.2.692-700.1982

| pmid = 6284708

| pmc = 220310

}}{{Cite journal

| last1 = Grisolia | first1 = V.

| last2 = Riccio | first2 = A.

| last3 = Bruni | first3 = C. B.

| title = Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon

| journal = Journal of Bacteriology

| volume = 155

| issue = 3

| pages = 1288–1296

| year = 1983

| doi = 10.1128/jb.155.3.1288-1296.1983

| pmid = 6309747

| pmc = 217827

}}

The firth step is catalysed instead by histadinolphosphate aminotransferase (encoded by hisC){{Cite journal

| last1 = Keseler | first1 = I. M.

| last2 = Collado-Vides | first2 = J.

| last3 = Santos-Zavaleta | first3 = A.

| last4 = Peralta-Gil | first4 = M.

| last5 = Gama-Castro | first5 = S.

| last6 = Muñiz-Rascado | first6 = L.

| last7 = Bonavides-Martinez | first7 = C.

| last8 = Paley | first8 = S.

| last9 = Krummenacker | first9 = M.

| last10 = Altman | first10 = T.

| last11 = Kaipa | first11 = P.

| last12 = Spaulding | first12 = A.

| last13 = Pacheco | first13 = J.

| last14 = Latendresse | first14 = M.

| last15 = Fulcher | first15 = C.

| last16 = Sarker | first16 = M.

| last17 = Shearer | first17 = A. G.

| last18 = MacKie | first18 = A.

| last19 = Paulsen | first19 = I.

| last20 = Gunsalus | first20 = R. P.

| last21 = Karp | first21 = P. D.

| title = EcoCyc: A comprehensive database of Escherichia coli biology

| doi = 10.1093/nar/gkq1143

| journal = Nucleic Acids Research

| volume = 39

| issue = Database issue

| pages = D583–D590

| year = 2010

| pmc = 3013716

| pmid = 21097882

}}

The peptide is 40.5kDa and associates to form a hexamer (unless truncated){{Cite journal

| last1 = Rangarajan | first1 = E. S.

| last2 = Proteau | first2 = A.

| last3 = Wagner | first3 = J.

| last4 = Hung | first4 = M. -N.

| last5 = Matte | first5 = A.

| last6 = Cygler | first6 = M.

| doi = 10.1074/jbc.M604916200

| title = Structural Snapshots of Escherichia coli Histidinol Phosphate Phosphatase along the Reaction Pathway

| journal = Journal of Biological Chemistry

| volume = 281

| issue = 49

| pages = 37930–37941

| year = 2006

| pmid = 16966333

| doi-access = free

}}

In E. coli hisB is found on the hisGDCBHAFI operon{{Cite journal

| last1 = Alifano | first1 = P.

| last2 = Carlomagno | first2 = M. S.

| last3 = Bruni | first3 = C. B.

| title = Location of the hisGDCBHAFI operon on the physical map of Escherichia coli

| journal = Journal of Bacteriology

| volume = 174

| issue = 11

| pages = 3830–3831

| year = 1992

| doi = 10.1128/jb.174.11.3830-3831.1992

| pmid = 1592835

| pmc = 206079

}}

The phosphatase activity possess a substrate ambiguity and overexpression of hisB can rescue phosphoserine phosphatase (serB) knockouts.{{Cite journal

| last1 = Patrick | first1 = W. M.

| last2 = Quandt | first2 = E. M.

| last3 = Swartzlander | first3 = D. B.

| last4 = Matsumura | first4 = I.

| title = Multicopy Suppression Underpins Metabolic Evolvability

| doi = 10.1093/molbev/msm204

| journal = Molecular Biology and Evolution

| volume = 24

| issue = 12

| pages = 2716–2722

| pmc = 2678898

| year = 2007

| pmid = 17884825

}}