Chorismate mutase, AroH class (IPR008243)
Short name: Chorismate_mutase_AroH
Chorismate mutase (CM; EC:22.214.171.124) catalyses the reaction at the branch point of the biosynthetic pathway leading to the three aromatic amino acids, phenylalanine, tryptophan and tyrosine (chorismic acid is the last common intermediate, and CM leads to the L-phenylalanine/L-tyrosine branch). It is part of the shikimate pathway, which is present only in bacteria, fungi and plants.
This entry represents a family of monofunctional (non-fused) chorismate mutases from Gram-positive bacteria (Firmicutes) and cyanobacteria. Trusted members of the family are found in operons with other enzymes of the chorismate pathways, both up- and downstream of CM (Listeria, Bacillus, Oceanobacillus) or are the sole CM in the genome where the other members of the chorismate pathways are found elsewhere in the genome (Nostoc, Thermosynechococcus). They are monofunctional, homotrimeric, nonallosteric enzymes and are not regulated by the end-product aromatic amino acids.
The three types of CM are AroQ class, prokaryotic type; AroQ class, eukaryotic type; and AroH class. They fall into two structural folds (AroQ class and AroH class) which are completely unrelated [PMID: 11528003]. The two types of the AroQ structural class (the Escherichia coli CM dimer and the yeast CM monomer) can be structurally superimposed, and the topology of the four-helix bundle forming the active site is conserved [PMID: 11528003].
- PD031888 (Chorismate_mutase_AroH)
- PS51167 (CHORISMATE_MUT_1)
- PF07736 (CM_1)
- PIRSF005965 (Chor_mut_AroH)
- PTHR21164 (PTHR21164)
- TIGR01796 (CM_mono_aroH)