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NAD(P)-binding domain-containing protein
Ornithine cyclodeaminase/mu-crystallin family
This family contains the bacterial Ornithine cyclodeaminase enzyme EC:4.3.1.12, which catalyses the deamination of ornithine to proline [1]. This family also contains mu-Crystallin the major component of the eye lens in several Australian marsupials, mRNA for this protein has also been found in human retina [2]. [1]. 2644238. Ornithine cyclodeaminase from octopine Ti plasmid Ach5: identification, DNA sequence, enzyme properties, and comparison with gene and enzyme from nopaline Ti plasmid C58. Schindler U, Sans N, Schroder J;. J Bacteriol 1989;171:847-854. [2]. 1384048. mu-crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina. Kim RY, Gasser R, Wistow GJ;. Proc Natl Acad Sci U S A 1992;89:9292-9296. (from Pfam)
Shikimate / quinate 5-dehydrogenase
This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate. Discusses the pentafunctional AROM multi-domain protein, which possesses a shikimate 5-dehydrogenase enzyme. The AROM protein catalyses steps two to six in the shikimate pathway in many microbial eukaryotes. [1]. 7556173. The molecular biology of multidomain proteins. Selected examples. Hawkins AR, Lamb HK;. Eur J Biochem 1995;232:7-18. (from Pfam)
ornithine cyclodeaminase family protein
ornithine cyclodeaminase family protein similar to Bacillus cereus delta(1)-pyrroline-2-carboxylate reductase, which catalyzes the reduction of delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, preferentially using NADPH over NADH as the electron donor
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