HMM Summary Page: TIGR01806

Functionputative chorismate mutase
Trusted Cutoff74.15
Domain Trusted Cutoff74.15
Noise Cutoff53.60
Domain Noise Cutoff53.60
Isology Typeequivalog
EC Number5.4.99.5
HMM Length114
Mainrole CategoryAmino acid biosynthesis
Subrole CategoryAromatic amino acid family
AuthorSelengut J
Entry DateJan 24 2003 9:28AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model represents a clade of probable chorismate mutases from alpha, beta and gamma proteobacteria as well as Mycobacterium tuberculosis and a clade of nematodes. Although the most likely function for the enzymes represented by this model is as a chorismate mutase, in no species are these enzymes the sole chorismate mutase in the genome. Also, in no case are these enzymes located in a region of the genome proximal to any other enzymes involved in chorismate pathways. Although the Pantoea enzyme has been shown to complement a CM-free mutant of E. coli [1], this was also shown to be the case with isochorismate-pyruvate lyase which only has a secondary (non-physiologically relevant) chorismate mutase activity [2]. This enzyme is believed to be a homodimer and be localized to the periplasm.
ReferencesRN [1] RM PMID: 8335631 RT The aroQ-encoded monofunctional chorismate mutase (CM-F) protein is a periplasmic enzyme in Erwinia herbicola. RA Xia T, Song J, Zhao G, Aldrich H, Jensen RA. RL J Bacteriol 1993 Aug;175(15):4729-37 RN [2] RM PMID: 11937513 RT Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities. RA Gaille C, Kast P, Haas D. RL J Biol Chem. 2002 Jun 14;277(24):21768-75.
Genome PropertyGenProp0039: phenylalanine biosynthesis from chorismate (HMM)
GenProp0045: tyrosine biosynthesis from chorismate (HMM)