|
|
2.9.1.1 |
Activity |
2.9.1.1 |
Description |
L-seryl-tRNA(Sec) selenium transferase |
Notes |
A family very distinct from all others, and composed solely of bacterial sequences.
Some sequences lacking the tRNA(Sec) binding domain are predicted to have a different function. Absence of tRNA(Sec) binding has been demonstrated for a homologous archaeal protein (see Kaiser J.T. et al., Biochemistry, 2005). |
PDB |
3W1J; |
PLP Fold Type |
I |
PLP-dependent Domain |
|
Number of sequences |
28 |
Sequences in seed alignment |
|
Reference sequence |
SELA_ECOLI |
Domain interval |
83-452 |
Catalytic site |
295 K |
| |
References |
Itoh Y1, Bröcker MJ, Sekine S, Hammond G, Suetsugu S, Söll D, Yokoyama S. (2013) Decameric SelA•tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation. Science. 340 75-8. Gursinsky, T.; Jager, J.; Andreesen, J. R.; Sohling, B. (2000) A selDABC cluster for selenocysteine incorporation in Eubacterium acidaminophilum Arch Microbiol 174 200-12. Tormay, P.; Wilting, R.; Lottspeich, F.; Mehta, P. K.; Christen, P.; Bock, A. (1998) Bacterial selenocysteine synthase--structural and functional properties Eur J Biochem 254 655-61. Forchhammer, K.; Leinfelder, W.; Boesmiller, K.; Veprek, B.; Bock, A. (1991) Selenocysteine synthase from Escherichia coli. Nucleotide sequence of the gene (selA) and purification of the protein J Biol Chem 266 6318-23. Articles on 2.9.1.1 |
last changed |
2017/07/11 17:09 |
|