InterPro : IPR013813

Name  Endoribonuclease L-PSP/chorismate mutase-like Short Name  Endoribo_LPSP/chorism_mut-like
Type  Domain Description  This entry represents the beta-alpha-beta-alpha-beta(2) domains common both to bacterial chorismate mutase and to members of the YjgF/Yer057p/UK114 family. These proteins form trimers with a three-fold symmetry with three closely-packed beta-sheets.Chorismate mutase (CM, ) is an enzyme of the aromatic amino acid biosynthetic pathway that catalyses the reaction at the branch point of the pathway leading to the three aromatic amino acids, phenylalanine, tryptophan and tyrosine (chorismic acid is the last common intermediate, and CM leads to the L-phenylalanine/L-tyrosine branch). It is part of the shikimate pathway, which is present only in bacteria, fungi and plants. The structure of chorismate mutase enzymes from Bacillus subtilis[]and Thermus thermophilushave been solved and were shown to have a catalytic homotrimer, with the active sites being located at the subunit interfaces, where residues from two subunits contribute to each site.The YjgF/Yer057p/UK114 family is a large, highly conserved, and widely distributed family of proteins found in bacteria, archaea and eukaryotes. YjgF (renamed RidA) deaminates reactive enamine/imine intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme reactions. The YjgF/YER057c/UK114 family of proteins is conserved in all domains of life suggesting that reactive enamine/imine metabolites are of concern to all organisms []. This family includes: YjgF and its orthologuesthe yeast growth inhibitor YER057cp that appears to play a role in the regulation of metabolic pathways and cell differentiation []the mammalian 14.5 kDa translational inhibitor protein UK114, also known as L-PSP (liver perchloric acid-soluble protein), with endoribonucleolytic activity that directly affects mRNA translation and can induce disaggregation of the reticulocyte polysomes into 80 S ribosomes []RutC from E. coli, which is essential for growth on uracil as sole nitrogen source and is thought to reduce aminoacrylate peracid to aminoacrylate []YabJ from B. subtilis, which is required for adenine-mediated repression of purine biosynthetic genes []Structurally these proteins are homotrimers with clefts between the monomeric subunits that are proposed to have some functional relevance [, , ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR019897 YjgF-like protein, conserved site YjgF-like_CS Conserved_site

0 Found In

0 Parent Features

9 Publications

First Author Title Year Journal Volume Pages
Lambrecht JA Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme reactions. 2012 J Biol Chem 287 3454-61
Sinha S Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family. 1999 Proc Natl Acad Sci U S A 96 13074-9
Morishita R Ribonuclease activity of rat liver perchloric acid-soluble protein, a potent inhibitor of protein synthesis. 1999 J Biol Chem 274 20688-92
Volz K A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli. 1999 Protein Sci 8 2428-37
Kim JM A member of the YER057c/yjgf/Uk114 family links isoleucine biosynthesis and intact mitochondria maintenance in Saccharomyces cerevisiae. 2001 Genes Cells 6 507-17
Deaconescu AM X-ray structure of Saccharomyces cerevisiae homologous mitochondrial matrix factor 1 (Hmf1). 2002 Proteins 48 431-6
Thakur KG Mycobacterium tuberculosis Rv2704 is a member of the YjgF/YER057c/UK114 family. 2010 Proteins 78 773-8
Kim KS The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. 2010 J Bacteriol 192 4089-102
Ladner JE The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer. 2000 Acta Crystallogr D Biol Crystallogr 56 673-83

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)