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InterPro: IPR020541 Chorismate synthase, conserved site

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1818 proteins

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Accession

IPR020541 Chorismate_synthase_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00787	CHORISMATE_SYNTHASE_1	1661
PROSITE pattern	PS00788	CHORISMATE_SYNTHASE_2	1637
PROSITE pattern	PS00789	CHORISMATE_SYNTHASE_3	1514
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000453 Chorismate synthase

GO Term annotation Help

Process

GO:0009073 aromatic amino acid family biosynthetic process

Function

GO:0004107 chorismate synthase activity

InterPro annotation

Entry Details in BioMart

Abstract

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.

This entry represents conserved regions from chorismate synthase that are rich in basic residues.

Structural links Help

PDB - click here

SCOP: d.258.1.1

Database links Help

Enzyme: EC:4.2.3.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR020541

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O02607 Chorismate synthase

O66493 Chorismate synthase

P23353 Chorismate synthase

P28777 Chorismate synthase

P57720 Chorismate synthase, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000453	Chorismate synthase
IPR020541	Chorismate synthase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Schaller A, Schmid J, Leibinger U, Amrhein N. Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers. J. Biol. Chem. 266 21434-8 1991 [PubMed: 1718979] http://intl.jbc.org/cgi/content/abstract/266/32/21434
2.	Jones DG, Reusser U, Braus GH. Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae. Mol. Microbiol. 5 2143-52 1991 [PubMed: 1837329] http://dx.doi.org/10.1111/j.1365-2958.1991.tb02144.x

Additional Reading Open in usermanual
	Viola CM, Saridakis V, Christendat D. Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology. Proteins 54 2004 166-9 [PubMed: 14705034] http://dx.doi.org/10.1002/prot.10592
	Quevillon-Cheruel S, Leulliot N, Meyer P, Graille M, Bremang M, Blondeau K, Sorel I, Poupon A, Janin J, van Tilbeurgh H. Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae. J. Biol. Chem. 279 2004 619-25 [PubMed: 14573601] http://dx.doi.org/10.1074/jbc.M310380200
	Maclean J, Ali S. The structure of chorismate synthase reveals a novel flavin binding site fundamental to a unique chemical reaction. Structure 11 2003 1499-511 [PubMed: 14656434] http://dx.doi.org/10.1016/j.str.2003.11.005
	Ahn HJ, Yoon HJ, Lee B 2nd, Suh SW. Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights. J. Mol. Biol. 336 2004 903-15 [PubMed: 15095868] http://dx.doi.org/10.1016/j.jmb.2003.12.072

InterPro 23.1