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2.6.1.37 |
Activity |
2.6.1.37 |
Description |
(2-aminoethyl)phosphonate--pyruvate aminotransferase |
Notes |
2-Aminoethylphosphonate (ciliatine) is the precursor of an array of phosphonated compounds (e.g., phosphonopolysaccharides), which are employed by some organisms for specialized functions such as chemical warfare, cell-cell communication, and host recognition. Enzymes in this family may be involved both in the synthesis and the degradation of ciliatine; their sequences are distantly related to those in the dhap aminotransferase family and to those of classic alanine-glyoxylate aminotransferases (family 2.6.1.44a).
Some biosynthetic enzymes (such as the enzyme from Treponema denticola) are part of bifunctional proteins containing also a N-terminal nucleotidyl transferase domain, which has been removed from the sequences included in the family. |
PDB |
1M32; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
17 |
Sequences in seed alignment |
|
Reference sequence |
T46947 |
Domain interval |
6-335 |
Catalytic site |
194 K |
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References |
Rice K, Batul K, Whiteside J, Kelso J, Papinski M, Schmidt E, Pratasouskaya A, Wang D, Sullivan R, Bartlett C, Weadge JT, Van der Kamp MW, Moreno-Hagelsieb G, Suits MD, Horsman GP
(2019) The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis Nat Commun 10 3698. Kim, A.D.; Baker, A.S.; Dunaway-Mariano, D.; Metcalf, W.W.; Wanner, B.L.; Martin, B.M.
(2002) The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway J Bacteriol 184 4134-40. Articles on 2.6.1.37 |
last changed |
2019/08/26 09:15 |
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