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lycopene cyclase domain-containing protein
lycopene cyclase domain-containing protein includes lycopene beta-cyclase which catalyzes the cyclization of both ends of lycopene to form beta-carotene, a retinal precursor
This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria [1] and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein [2], where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly.
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