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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

Number of sequences
17
Sequences in seed alignment
BacteriaNP_437517 (Sinorhizobium meliloti); AE004560_7 (Pseudomonas aeruginosa PA01); CAD24488 (Pseudomonas putida); AAP08310 (Bacillus cereus); NP_655226 (Bacillus anthracis A2012); ZP_00083884 (Pseudomonas fluorescens); ZP_00035195 (Enterococcus faecium); NP_972021 (Treponema denticola ATCC 35405); ZP_00028959 (Burkholderia fungorum); CAD63312 (Lactobacillus plantarum WCFS1); WP_103599669 (Campylobacter concisus); YP_002773978 (Brevibacillus brevis NBRC 100599); T46947 (Salmonella typhimurium); WP_010255470 (Treponema primitia); WP_045519162 (Bacillus niacini); H82437 (Vibrio cholerae);
Other_EukaryaNP_859432 (Leishmania major);

DISPLAY: Fasta format, alignment, hmm, hmm_local


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