CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1420 | set domain protein methyltransferase, domain 2 |
|
3.90.1420.10 | Rubisco LSMT, substrate-binding domain |
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 | 1MLV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure and catalytic mechanism of a SET domain protein methyltransferase.
Cell(Cambridge,Mass.)
|
