Sequence
ATGATCCTCACCGAAGACCAGATCACCGGCTACCGGGAGAACGGCTACCTCGTCGTCGACCGGCTGTTCAACACCGAAGAGGTCGACGCGTTGCGTGACGCGTTCGCGCGGGACGGCGAAATCCCCGGCGACCAGCGGATCGCCGAGAACGACGGCGAAGACGTCCGCGCGATCTACGCCTCCCACCTCCGGCAACCCGAGTTCGCCCGGCTGGTCCGCTCCCCCAGGCTGCTCGGCCCGGTGCGACAGCTGCTGACCGACAAGGTGTACGTCTACCAGTTCAAGATCAACGCCAAGCCGGCGTTCGTCGGCGGTGGCTGGGCGTGGCACCAGGACTTCACCGCGTGGCGGATCGCCGACGCCCTGCCCGAGCCCAAGCTGGTCAACGTCGGGCTGTTCCTCGACGACGTCACCGAGTTCAACGGCCCGCTGATGTTCGTGCCCGGCTCACACCGGCACGGGTTGATCCGGTCGGACCGCGGCGGCACGATGAAGTCCATGCAGCATCTGGACCCGGACGACATCCAGCTGACCACGACCGAGATGGCCGGTCTCGTCCGGCGATGCGGCATGGACAGCCCCAAGGGCCTGGCCGGTTCGGTGATCTTCTTCGACCCGGAGATCGTGCACGGCTCGGCCACCAACATGTCGCCCTTCAGCCGCCGGCTGCTGTTGGTGACGTACAACGACAGCACGAACGCTCCACTGGGCACGCCCCGAGAGTGGTACCTGGTCGAACAGGACACCACCGCGTTGGAGATCGTCGACGAACCTTTGCTGGCCCTCCGGTGA
The phyH gene from the uncultured bacterium Esnapd2 encodes a phytanoyl-CoA dioxygenase that catalyzes the stereospecific hydroxylation of L-proline to form trans-4-hydroxy-L-proline. A synthetic mutant carrying the L170A and P172N substitutions exhibits enhanced hydroxylation activity toward L-proline compared with the wild-type enzyme, indicating that targeted residue modifications can improve substrate conversion efficiency [212].
| Gene size: | |
| Protein size: | |
| Reactions | R1791 |
| Compounds affected | trans-4-hydroxy-L-proline |
Databases
| EraGene: | 2197612 |
|---|---|
| GenBank: | AGS49339.1 |