HMM Summary Page: TIGR01803

Functionchorismate mutase related enzymes
Trusted Cutoff73.35
Domain Trusted Cutoff73.35
Noise Cutoff60.35
Domain Noise Cutoff60.35
Isology Typesubfamily
HMM Length82
Gene Ontology TermGO:0003824: catalytic activity molecular_function
GO:0008152: metabolic process biological_process
AuthorSelengut J
Entry DateJan 22 2003 2:20PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis subfamily includes two enzymes which are variants on the mechanism of chorismate mutase and are likely to have evolved from an ancestral chorismate mutase enzyme. 4-amino-4-deoxy-chorismate mutase produces amino-deoxy-prephenate which is subsequently converted to para-dimethylamino-phenylalanine, a component of the natural product pristinamycin [1]. Isochorismate-pyruvate lyase presumably catalyzes the same type of 2+2+2 cyclo-rearrangement as chorismate mutase, but acting on isochorismate, this results in two broken bonds instead of one broken and one made. The product of this reaction is salicylate (2-hydroxy-benzoate) which is also incorporated into various natural products [2].
ReferencesRN [1] RM PMID: 9044253 RT Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-phenylalanine precursor of pristinamycin I. RA Blanc V, Gil P, Bamas-Jacques N, Lorenzon S, Zagorec M, Schleuniger J, Bisch D, Blanche F, Debussche L, Crouzet J, Thibaut D. RL Mol Microbiol 1997 Jan;23(2):191-202 RN [2] RM PMID: 7500944 RT Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa. RA Serino L, Reimmann C, Baur H, Beyeler M, Visca P, Haas D. RL Mol Gen Genet 1995 Nov 15;249(2):217-28