Aquifex aeolicus VF5 Pathway: histidine biosynthesis
Inferred by computational analysis

Pathway diagram: histidine biosynthesis

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Superclasses: BiosynthesisAmino Acids BiosynthesisProteinogenic Amino Acids BiosynthesisL-histidine Biosynthesis

Pathway Summary from MetaCyc:
The genes necessary for histidine biosynthesis have been identified in many bacteria, fungi, plants, and archaea. The pathway in all of these organisms is identical, with small differences in some of the enzymes used. Histidine is an essential amino acid, and is not synthesized by mammals.

A few differences between different organisms concern whether the enzymes are mono- or bifunctional. One such case is the enzyme histidinol-phosphate phosphatase (EC Some organisms, including Escherichia coli K-12, Salmonella enterica enterica serovar Typhimurium and Haemophilus influenzae, have a bifunctional enzyme, with the C-terminal domain exhibiting imidazoleglycerol-phosphate dehydratase (EC activity. These enzymes belong to the DDDD phosphohydrolase/phosphotransferase superfamily. Other organisms have separate monofunctional enzymes catalyzing these two reactions. Monofunctional histidinol-phosphate phosphatases belong to either the PHP (polymerase and histidinol phosphatase) superfamily, as in the case of Bacillus subtilis, Saccharomyces cerevisiae and Thermus thermophilus HB8 [Omi04], or to the DDDD superfamily, as in the case of the archaeon Thermococcus onnurineus NA1 [Lee08].

Another such case concerns the conversion of phosphoribulosylformimino-AICAR-P (BBM III) to D-erythro-imidazole-glycerol-phosphate (IGP) and 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (AICAR). This process requires two catalytic functions, including the transfer of an amide from L-glutamine and a cyclization reaction. In prokaryotes, these two catalytic activities are encoded by two genes whose products form a complex. In yeast and plants, this conversion is catalyzed by a single bifunctional enzyme.

In all organisms operating the pathway, the enzyme catalyzing the first step is feedback-inhibited by L-histidine. In plants, the entire pathway is located inside the chloroplast [Stepansky06].

Pathway Evidence Glyph:

Pathway evidence glyph

This organism is in the expected taxonomic range for this pathway.

Key to pathway glyph edge colors:

  An enzyme catalyzing this reaction is present in this organism
  An enzyme catalyzing this reaction was identified in this organism by the Pathway Hole Filler
  The reaction is unique to this pathway in MetaCyc

Revised in MetaCyc 10-Oct-2008 by Caspi R, SRI International
Imported from MetaCyc 08-Aug-2014 by Subhraveti P, SRI International


Lee08: Lee HS, Cho Y, Lee JH, Kang SG (2008). "Novel monofunctional histidinol-phosphate phosphatase of the DDDD superfamily of phosphohydrolases." J Bacteriol 190(7);2629-32. PMID: 18223080

Omi04: Omi R, Goto M, Nakagawa N, Miyahara I, Hirotsu K (2004). "Expression, purification and preliminary X-ray characterization of histidinol phosphate phosphatase." Acta Crystallogr D Biol Crystallogr 60(Pt 3);574-6. PMID: 14993698

Stepansky06: Stepansky A, Leustek T (2006). "Histidine biosynthesis in plants." Amino Acids 30(2);127-42. PMID: 16547652

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Green04: Green ML, Karp PD (2004). "A Bayesian method for identifying missing enzymes in predicted metabolic pathway databases." BMC Bioinformatics 5;76. PMID: 15189570

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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Page generated by Pathway Tools version 20.0 (software by SRI International) on Fri May 6, 2016, BIOCYC12.