UniProt functional annotation for Q43088



	UniProt functional annotation for Q43088

UniProt code: Q43088.

Organism: Pisum sativum (Garden pea).

Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.

Function: Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase. {ECO:0000269|PubMed:22547063}.

Catalytic activity: Reaction=L-lysyl-[ribulose-1,5-bisphosphate carboxylase] + 3 S- adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl- [ribulose-1,5-bisphosphate carboxylase] + 3 S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:50996, Rhea:RHEA-COMP:12858, Rhea:RHEA- COMP:12859, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.127;

Catalytic activity: Reaction=[fructose-bisphosphate aldolase]-L-lysine + 3 S-adenosyl-L- methionine = [fructose-bisphosphate aldolase]-N(6),N(6),N(6)- trimethyl-L-lysine + 3 H(+) + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51000, Rhea:RHEA-COMP:12861, Rhea:RHEA-COMP:12862, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.259;

Biophysicochemical properties: Kinetic parameters: KM=12.9 uM for fructose-bisphosphate aldolase 2 {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; KM=14.0 uM for fructose-bisphosphate aldolase 3 {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; KM=32.0 uM for gamma-tocopherol methyltransferase {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; KM=4.5 uM for rubisco {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; KM=6 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; Vmax=19.5 nmol/min/mg enzyme with fructose-bisphosphate aldolase 2 as substrate {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; Vmax=9.0 nmol/min/mg enzyme with fructose-bisphosphate aldolase 3 as substrate {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; Vmax=1.7 nmol/min/mg enzyme with gamma-tocopherol methyltransferase as substrate {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; Vmax=44.6 nmol/min/mg enzyme with rubisco as substrate {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; Vmax=56 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; Note=Kcat is 0.047 sec(-1) for S-adenosyl-L-methionine. Kcat is 0.038 sec(-1) for rubisco.;

Subunit: Homotrimer. {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:12819771, ECO:0000269|PubMed:16682405}.

Subcellular location: Plastid, chloroplast.

Tissue specificity: Highly expressed in leaf.

Similarity: Belongs to the class V-like SAM-binding methyltransferase superfamily. Plant protein-lysine LSMT methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00916}.

Annotations taken from UniProtKB at the EBI.


Organism:		Pisum sativum (Garden pea).
Taxonomy:		Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.



Function:		Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase. {ECO:0000269\|PubMed:22547063}.


Catalytic activity:		Reaction=L-lysyl-[ribulose-1,5-bisphosphate carboxylase] + 3 S- adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl- [ribulose-1,5-bisphosphate carboxylase] + 3 S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:50996, Rhea:RHEA-COMP:12858, Rhea:RHEA- COMP:12859, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.127;
Catalytic activity:		Reaction=[fructose-bisphosphate aldolase]-L-lysine + 3 S-adenosyl-L- methionine = [fructose-bisphosphate aldolase]-N(6),N(6),N(6)- trimethyl-L-lysine + 3 H(+) + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51000, Rhea:RHEA-COMP:12861, Rhea:RHEA-COMP:12862, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.259;
Biophysicochemical properties:		Kinetic parameters: KM=12.9 uM for fructose-bisphosphate aldolase 2 {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; KM=14.0 uM for fructose-bisphosphate aldolase 3 {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; KM=32.0 uM for gamma-tocopherol methyltransferase {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; KM=4.5 uM for rubisco {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; KM=6 uM for S-adenosyl-L-methionine {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; Vmax=19.5 nmol/min/mg enzyme with fructose-bisphosphate aldolase 2 as substrate {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; Vmax=9.0 nmol/min/mg enzyme with fructose-bisphosphate aldolase 3 as substrate {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; Vmax=1.7 nmol/min/mg enzyme with gamma-tocopherol methyltransferase as substrate {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; Vmax=44.6 nmol/min/mg enzyme with rubisco as substrate {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; Vmax=56 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:22547063}; Note=Kcat is 0.047 sec(-1) for S-adenosyl-L-methionine. Kcat is 0.038 sec(-1) for rubisco.;
Subunit:		Homotrimer. {ECO:0000269\|PubMed:12372303, ECO:0000269\|PubMed:12819771, ECO:0000269\|PubMed:16682405}.
Subcellular location:		Plastid, chloroplast.
Tissue specificity:		Highly expressed in leaf.
Similarity:		Belongs to the class V-like SAM-binding methyltransferase superfamily. Plant protein-lysine LSMT methyltransferase family. {ECO:0000255\|PROSITE-ProRule:PRU00916}.