|Function||putative chorismate mutase|
|Domain Trusted Cutoff||74.15|
|Domain Noise Cutoff||53.60|
|Mainrole Category||Amino acid biosynthesis|
|Subrole Category||Aromatic amino acid family|
|Entry Date||Jan 24 2003 9:28AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||This 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 , this was also shown to be the case with isochorismate-pyruvate lyase which only has a secondary (non-physiologically relevant) chorismate mutase activity . This enzyme is believed to be a homodimer and be localized to the periplasm.|
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
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 Property||GenProp0039: phenylalanine biosynthesis from chorismate (HMM)|
| ||GenProp0045: tyrosine biosynthesis from chorismate (HMM)|
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