Activities | Families | Sequences | Fold types | References | Help
B6db families: 2.6.1.37

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
Domain alignment
Domain hmm
Fold type I

Reference sequence T46947
Domain interval 6-335
Catalytic site 194 K
 
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

B6db families