CATH Classification

Domain Context

CATH Clusters

Superfamily Rubisco LSMT, substrate-binding domain
Functional Family Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic

Enzyme Information

2.1.1.127
[Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase.
based on mapping to UniProt Q43088
3 S-adenosyl-L-methionine + [ribulose-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-bisphosphate carboxylase]- N(6),N(6),N(6)-trimethyl-L-lysine.
-!- The enzyme catalyzes three successive methylations of Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate- carboxylase (EC 4.1.1.39). -!- Only the three methylated form is observed. -!- The enzyme from pea (Pisum sativum) also three-methylates a specific lysine in the chloroplastic isoforms of fructose-bisphosphate aldolase (EC 4.1.2.13).
2.1.1.259
[Fructose-bisphosphate aldolase]-lysine N-methyltransferase.
based on mapping to UniProt Q43088
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]- N(6),N(6),N(6)-trimethyl-L-lysine.
-!- The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13). -!- The enzyme from pea (Pisum sativum) also methylates Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate- carboxylase (EC 4.1.1.39), but that from Arabidopsis thaliana does not.

UniProtKB Entries (1)

Q43088
RBCMT_PEA
Pisum sativum
Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic

PDB Structure

PDB 2H2J
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
Couture, J.F., Hauk, G., Thompson, M.J., Blackburn, G.M., Trievel, R.C.
J.Biol.Chem.