PROSITE documentation PDOC00628Chorismate synthase signatures
Chorismate synthase (EC 4.2.3.5) catalyzes the last of the seven steps in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans elimination of the phosphate group from 5-enolpyruvylshikimate-3-phosphate (EPSP) to form chorismate which can then be used in phenylalanine, tyrosine or tryptophan biosynthesis. Chorismate synthase requires the presence of a reduced flavin mononucleotide (FMNH2 or FADH2) for its activity.
Chorismate synthase from various sources shows [1,2] a high degree of sequence conservation. It is a protein of about 360 to 400 amino-acid residues. We developed three signature patterns from conserved regions rich in basic residues (mostly arginines). The first is in the N-terminal section, the second is central and the third is C-terminal.
Last update:April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Schaller A. Schmid J. Leibinger U. Amrhein N. |
| Title | Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers. | |
| Source | J. Biol. Chem. 266:21434-21438(1991). | |
| PubMed ID | 1718979 |
| 2 | Authors | Jones D.G.L. Reusser U. Braus G.H. |
| Title | Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae. | |
| Source | Mol. Microbiol. 5:2143-2152(1991). | |
| PubMed ID | 1837329 |
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