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Homocitrate synthase post-HMGL domain-like
HMGL-like
This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase. (from Pfam)
Lrp/AsnC ligand binding domain-containing protein
The l-leucine-responsive regulatory protein (Lrp/AsnC) family is a family of similar bacterial transcription regulatory proteins. The family is named after two E. coli proteins involved in regulating amino acid metabolism. This entry corresponds to the usually C-terminal regulatory ligand binding domain. Structurally this domain has a dimeric alpha/beta barrel fold [2]. This domain binds almost exclusively amino acids but also 4-hydroxyphenylpyruvate and kynurenine (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 7770911. The eubacterial transcriptional activator Lrp is present in the. archaeon Pyrococcus furiosus.. Kyrpides NC, Ouzounis CA;. Trends Biochem Sci 1995;20:140-141.. [2]. 17374605. The structure and transcriptional analysis of a global regulator. from Neisseria meningitidis.. Ren J, Sainsbury S, Combs SE, Capper RG, Jordan PW, Berrow NS,. Stammers DK, Saunders NJ, Owens RJ;. J Biol Chem. 2007;282:14655-14664. (from Pfam)
2-isopropylmalate synthase
2-isopropylmalate synthase converts acetyl-CoA and alpha-ketoisovalerate into alpha-isopropylmalate in the committed step of leucine biosynthesis
homocitrate synthase
This model includes the yeast LYS21 gene which carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway. A related pathway is found in Thermus thermophilus [1]. This enzyme is closely related to 2-isopropylmalate synthase (LeuA) and citramalate synthase (CimA), both of which are present in the euryarchaeota. Some archaea have a separate homocitrate synthase (AksA) which also synthesizes longer homocitrate analogs [2].
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