HMM Summary Page: TIGR03540

FunctionLL-diaminopimelate aminotransferase
Trusted Cutoff593.25
Domain Trusted Cutoff593.25
Noise Cutoff583.30
Domain Noise Cutoff583.30
Isology Typehypoth_equivalog
EC Number2.6.1.83
HMM Length383
AuthorSelengut J
Entry DateFeb 6 2008 9:48AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis clade of the PF00155 superfamily of aminotransferases includes several which are adjacent to elements of the lysine biosynthesis via diaminopimelate pathway (GenProp0125). Every member of this clade is from a genome which possesses most of the lysine biosynthesis pathway but lacks any of the known aminotransferases, succinylases, desuccinylases, acetylases or deacetylases typical of the acylated versions of this pathway nor do they have the direct, NADPH-dependent enzyme (ddh). Although there is no experimental characterization of any of the sequences in this clade, a direct pathway is known in plants and Chlamydia [1, 2] and the clade containing the Chlamydia gene is a neighboring one in the same PF00155 superfamily so it seems quite reasonable that these enzymes catalyze the same transformation.
ReferencesRN [1] RM PMID:17583737 RT Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. RA Watanabe N, Cherney MM, van Belkum MJ, Marcus SL, Flegel MD, Clay MD, Deyholos MK, Vederas JC, James MN RL J Mol Biol. 2007 Aug 17;371(3):685-702. Epub 2007 May 26. RN [2] RM PMID:17093042 RT L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine. RA McCoy AJ, Adams NE, Hudson AO, Gilvarg C, Leustek T, Maurelli AT RL Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17909-14. Epub 2006 Nov 8.
Genome PropertyGenProp0125: lysine biosynthesis via diaminopimelate (DAP) (HMM)