Structural highlights
Function[RIDA_BACSU] Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis. May have a role in the purine metabolism.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe yabJ gene in Bacillus subtilis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein. The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical function. The 1.7-A crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity. The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins. Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family.,Sinha S, Rappu P, Lange SC, Mantsala P, Zalkin H, Smith JL Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13074-9. PMID:10557275[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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