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    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)

    Date:
    2024-10-16
    Family Accession:
    NF013224.5
    Method:
    HMM

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