Entry
Name
[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase;
rubisco methyltransferase;
ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase;
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase;
S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase;
RuBisCO methyltransferase;
RuBisCO LSMT
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine N6-methyltransferase
Reaction(IUBMB)
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine [RN:
R05179 ]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:
C00019 ];
[ribulose-1,5-bisphosphate carboxylase]-L-lysine [CPD:
C06403 ]
Product
S-adenosyl-L-homocysteine [CPD:
C00021 ];
[ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine [CPD:
C06404 ]
Comment
The enzyme catalyses 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 [3]. 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 ) [5].
History
EC 2.1.1.127 created 1999, modified 2012
Orthology
K00592 [ribulose-bisphosphate carboxylase]/[fructose-bisphosphate aldolase]-lysine N-methyltransferase
Genes
CSAT : 104740061 104755697 104772851
HSYR : 120169338 120210702
EGR : 104422322 104434604 104453926 104453927 120293321
PVU : PHAVU_002G169400g PHAVU_005G037700g
LJA : Lj4g3v0684250.2(Lj4g3v0684250.2)
LANG : 109339197 109349547
CMAX : 111471356 111471861
CMOS : 111450646 111454704
CPEP : 111799237 111805617 111805618
SPEN : 107020229 107020231
SSTN : 125866777 125867676
CANN : 107847854 107848269
NTA : 107778201(RBCMT) 107809813
CSIN : 114264208 114306448
ATRI : 130809122 130820119
PSOM : 113299904 113300303
DOSA : Os09t0411650-01(Os09g0411650)
TAES : 123103906 123114815 123121680
SMO : SELMODRAFT_119151 SELMODRAFT_449995
VCN : VOLCADRAFT_109735(VRMT1)
MPP : MICPUCDRAFT_36635(JGI:MicpuC2_36635)
» show all
Taxonomy
Reference
Authors
Wang P, Royer M, Houtz RL.
Title
Affinity purification of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase.
Journal
Reference
Authors
Ying Z, Janney N, Houtz RL
Title
Organization and characterization of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase gene in tobacco.
Journal
Sequence
Reference
Authors
Dirk LM, Flynn EM, Dietzel K, Couture JF, Trievel RC, Houtz RL
Title
Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases.
Journal
Reference
Authors
Magnani R, Nayak NR, Mazarei M, Dirk LM, Houtz RL
Title
Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase.
Journal
Reference
Authors
Mininno M, Brugiere S, Pautre V, Gilgen A, Ma S, Ferro M, Tardif M, Alban C, Ravanel S
Title
Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 2.1.1.127