SMART: CM_2 domain annotation

CM_2 Chorismate mutase type II

SMART accession number:	SM00830
Description:	Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine (PUBMED:9642265), (PUBMED:9497350).
Family alignment:	View or

There are 858 CM_2 domains in 858 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Schnappauf G, Krappmann S, Braus GH
- Tyrosine and tryptophan act through the same binding site at the dimerinterface of yeast chorismate mutase.
- J Biol Chem. 1998; 273: 17012-7
- Display abstract
- Tyrosine and tryptophan are the regulators of the dimeric yeast chorismatemutase. Biochemical studies reveal two binding sites per molecule for botheffectors, tyrosine or tryptophan. A single binding site is built up byhelix 8 and helices 4 and 5 of two different subunits. The binding siteshave been analyzed in the active enzyme by site directed mutagenesis ofcritical codons of the coding gene, ARO7. Gly-141 and Ser-142, which bothreside on helix 8, are involved in the binding of tyrosine or tryptophanpresumably by interacting specifically with the amino- andcarboxylate-groups of these amino acid effectors. Interaction with Thr-145of helix 8 is required for a strong tyrosine binding to the allostericsite. Replacement of Arg-75, which connects helices 4 and 5 or of Arg-76,which is part of helix 5 by alanine residues, resulted in unregulatedenzymes. These two residues are bonded to the carboxylate group andphenolic hydroxyl group of tyrosine, respectively, but do not interactwith tryptophan by hydrogen bonding in the crystal structures.Phenylalanine, which has low binding affinity slightly activated thechorismate mutase. A T145V mutant chorismate mutase, however, showedincreased activation by phenylalanine. Our results support a mechanism bywhich tyrosine contracts the allosteric site by interacting with itsphenolic hydroxyl group. Tryptophan works in an inverse way by opening theallosteric site through the steric size of its side chain.
- Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B
- Chorismate mutase-prephenate dehydratase from Escherichia coli. Study ofcatalytic and regulatory domains using genetically engineered proteins.
- J Biol Chem. 1998; 273: 6248-53
- Display abstract
- The bifunctional P-protein, which plays a central role in Escherichia coliphenylalanine biosynthesis, contains two catalytic domains (chorismatemutase and prephenate dehydratase activities) as well as one R-domain (forfeedback inhibition by phenylalanine). Six genes coding for P-proteindomains or subdomains were constructed and successfully expressed.Proteins containing residues 1-285 and residues 1-300 retained full mutaseand dehydratase activity, but exhibited no feedback inhibition. Proteinscontaining residues 101-386 and residues 101-300 retained full dehydrataseactivity, but lacked mutase activity. Fluorescence emission spectra andbinding assays indicated that residues 286-386 were crucial forphenylalanine binding. The mutase (residues 1-109), dehydratase (residues101-285), and regulatory (residues 286-386) activities were thus shown toreside in discrete domains of the P-protein. Both the mutase domain andthe native P-protein formed dimers. Deletion of the mutase domaindiminished phenylalanine binding to the regulatory site as well asprephenate binding to the dehydratase domain, both through cooperativeeffects. Besides eliminating feedback inhibition, removal of the R-domaindecreased the affinity of chorismate mutase for chorismate.
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

Links (links to other resources describing this domain)
PFAM CM_2

PDB code	Main view	Title
1ecm		Atomic structure of the buried catalytic pocket of escherichia coli chorismate mutase
1ybz		Conserved hypothetical protein from pyrococcus furiosus pfu- 1581948-001
2ao2		The 2.07 angstrom crystal structure of mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions
2d8d		Structure of chorismate mutase (form i) from thermus thermophilus hb8
2d8e		Structure of chorismate mutase (form ii) from thermus thermophilus hb8
2f6l		X-ray structure of chorismate mutase from mycobacterium tuberculosis
2fp1		Secreted chorismate mutase from mycobacterium tuberculosis
2fp2		Secreted chorismate mutase from mycobacterium tuberculosis
2gbb		Crystal structure of secreted chorismate mutase from yersinia pestis
2gtv		Nmr structure of monomeric chorismate mutase from methanococcus jannaschii
2h9c		Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa
2h9d		Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa
2qbv		Crystal structure of intracellular chorismate mutase from mycobacterium tuberculosis
2vkl		X-ray crystal structure of the intracellular chorismate mutase from mycobactrerium tuberculosis in complex with malate
2w19
2w1a
3hgw
3hgx

CM_2

3D Structures of CM_2 domains in PDB