| Accession | TIGR01806 |
| Name | CM_mono2 |
| Function | putative chorismate mutase |
| Trusted Cutoff | 74.15 |
| Domain Trusted Cutoff | 74.15 |
| Noise Cutoff | 53.60 |
| Domain Noise Cutoff | 53.60 |
| Isology Type | equivalog |
| EC Number | 5.4.99.5 |
| HMM Length | 114 |
| Mainrole Category | Amino acid biosynthesis |
| Subrole Category | Aromatic amino acid family |
| Author | Selengut J |
| 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 [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. |
| References | RN [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 Property | GenProp0039: phenylalanine biosynthesis from chorismate (HMM) |
| | GenProp0045: tyrosine biosynthesis from chorismate (HMM) |
