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Information on EC 2.1.1.259 - [fructose-bisphosphate aldolase]-lysine N-methyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9XI84

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IUBMB Comments
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.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9XI84
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
3
+
[fructose-bisphosphate aldolase]-L-lysine
=
3
+
[fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
Synonyms
pslsmt, chloroplastic protein methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chloroplastic protein methyltransferase
-
protein-lysine methyltransferase-like
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-
Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase
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-
-
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Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase
-
-
-
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Rubisco methyltransferase
-
-
-
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S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[fructose-bisphosphate aldolase]-lysine N6-methyltransferase
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) [2], but that from Arabidopsis thaliana does not.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine394
3 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine394
show the reaction diagram
-
-
-
?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine
S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
-
the substrate is trimethylated at a conserved lysyl residue located close to the C terminus
-
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
-
no natural substrate. The enzyme is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive
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-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine
S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
-
the substrate is trimethylated at a conserved lysyl residue located close to the C terminus
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants, overview. The His-Ala/Pro-Trp triad located in the central part of LSMT enzymes is the key motif to confer the capacity to trimethylate Rubisco. Two of the critical residues are located on a surface loop outside the methyltransferase catalytic site. A strict correlation between the presence of the triad motif and the in vivo methylation status of Rubisco is observed, distribution of the motif into a phylogenetic tree, overview. Chloroplastic fructose-1,6-bisphosphate aldolases (FBAs) are naturally trimethylated in both Pisum sativum and Arabidopsis thaliana, whereas the Rubisco large subunit is trimethylated only in the former species. The distribution of the motif into a phylogenetic tree further suggests that the ancestral function of LSMT was FBA trimethylation. In a recent event during higher plant evolution, this function evolved in ancestors of Fabaceae, Cucurbitaceae, and Rosaceae to include Rubisco as an additional substrate to the archetypal enzyme
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RBCMT_ARATH
482
0
54612
Swiss-Prot
Chloroplast (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
247H/Ins254A/R259W
mutant is able to methylate both Rubisco and fructose 1,6-bisphosphate aldolase with similar efficiency
I242V
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
Ins254A
enzyme is able to methylate Rubisco in addition to fructose 1,6-bisphosphate aldolase
Ins254A/R259W
mutation enhances methylation of Rubisco without altering fructose 1,6-bisphosphate aldolase methylation
P240A
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
R259W
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
S299P
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
V269L
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
Y247H
mutant is not able to methylate Rubisco, activity is severely impaired
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged chimeric enzyme mutants from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
sequence comparisons and phylogenetic tree, recombinant expression of His-tagged chimeric enzyme mutants in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mininno, M.; Brugiere, S.; Pautre, V.; Gilgen, A.; Ma, S.; Ferro, M.; Tardif, M.; Alban, C.; Ravanel, S.
Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants
J. Biol. Chem.
287
21034-21044
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
Ma, S.; Martin-Laffon, J.; Mininno, M.; Gigarel, O.; Brugiere, S.; Bastien, O.; Tardif, M.; Ravanel, S.; Alban, C.
Molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants
Mol. Plant
9
569-581
2016
Arabidopsis thaliana (Q9XI84), Arabidopsis thaliana, Pisum sativum (Q43088), Pisum sativum
Manually annotated by BRENDA team