KEGG   ENZYME: 2.1.1.259
Entry
EC 2.1.1.259                Enzyme                                 
Name
[fructose-bisphosphate aldolase]-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
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:[fructose-bisphosphate aldolase]-lysine N6-methyltransferase
Reaction(IUBMB)
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
Substrate
S-adenosyl-L-methionine [CPD:C00019];
[fructose-bisphosphate aldolase]-L-lysine [CPD:C21364]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
[fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine [CPD:C21365]
Comment
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.
History
EC 2.1.1.259 created 2012
Orthology
K00592  [ribulose-bisphosphate carboxylase]/[fructose-bisphosphate aldolase]-lysine N-methyltransferase
Genes
ATEN116294947
PDAM113668217
ATHAT1G14030(LSMT-L)
ALY9326099
CRB17896815
CSAT104740061 104755697 104772851
EUSEUTSA_v10007614mg
BRP103843008
BNA106369122 106415812
BOE106307554
RSZ108806159
THJ104801808
CPAP110814551
CIT102629962
CICCICLE_v10031325mg
PVY116120564
MINC123213207
TCC18610345
GRA105794210
GHI107887371 107910114
GAB108483107
DZI111318315
EGR104422322 104434604 104453926 104453927
GMX100801721 100818113
GSJ114403778 114419860
PVUPHAVU_002G169400g PHAVU_005G037700g
VRA106766684
VAR108345304
VUN114177883
CCAJ109790121
APRC113858026
MTR25492966
CAM101490590
PSAT127108354
LJALj4g3v0684250.2(Lj4g3v0684250.2)
ADU107481199
AIP107631855
AHF112734120 112791958
LANG109339197 109349547
FVE101298121
RCN112197725
PPER18793936
PMUM103321538
PAVI110751405
PDUL117633227
MDM103425473
PXB103947201
ZJU107428930
MNT21398778
CSV101205332
CMO103485765
BHJ120080317
MCHA111023237
CMAX111471356 111471861
CMOS111450646 111454704
CPEP111799237 111805617 111805618
RCU8281847
JCU105630482
HBR110651139 110652291
MESC110625317
POP7498187
PEU105121014
PALZ118062350
JRE108992916
QSU112002850
QLO115978779
TWL120001376
VVI100243771
VRI117912770
SLY101259632
SPEN107020229 107020231
SOT102587278 102587919
SSTN125866777 125867676
CANN107847854 107848269
NTA107778201(RBCMT) 107809813
NSY104226426
NTO104089653
NAU109214572
INI109161120
ITR116004215
SIND105159997
OEU111398907
EGT105967526
SSPL121798072
APAN127261740
HAN110911425
ECAD122578954
LSV111879053
CCAV112527798
DCR108202653
CSIN114264208 114306448
BVG104897864
SOE110785063
CQI110706360 110712993
NNU104598072
MING122076876
TSS122654711
PSOM113299904 113300303
OSA9266797
DOSAOs09t0411650-01(Os09g0411650)
OBR102703061
BDI100823096
ATS109773851
TDC119301750 119309640
TAES123103906 123114815 123121680
TUA125509474
LPER127301336
SBI8063304
ZMA100382373
SITA101771156
SVS117845324
PVIR120660633
PHAI112883419
PDA103714847
EGU105058571
MUS103992431 103992436
ZOF121969188 121974301
DCT110107875
PEQ110025947
AOF109826056
NCOL116248103
ATR18422052
SMOSELMODRAFT_119151 SELMODRAFT_449995
PPP112279922
CRECHLRE_16g661350v5
VCNVOLCADRAFT_109735(VRMT1)
MNGMNEG_7683
CSLCOCSUDRAFT_19420
CVRCHLNCDRAFT_8187
OLUOSTLU_43434
OTAOT_ostta14g00200
BPGBathy04g04850
MISMICPUN_63742
MPPMICPUCDRAFT_36635
CMECYME_CMJ178C
GSLGasu_15050
CCPCHC_T00002187001
NGDNGA_2061300
PIFPITG_00531
PSOJPHYSODRAFT_561468
SPARSPRG_03390
EHXEMIHUDRAFT_448733
 » show all
Reference
1  [PMID:17635932]
  Authors
Magnani R, Nayak NR, Mazarei M, Dirk LM, Houtz RL
  Title
Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase.
  Journal
J Biol Chem 282:27857-64 (2007)
DOI:10.1074/jbc.M702069200
Reference
2  [PMID:22547063]
  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
J Biol Chem 287:21034-44 (2012)
DOI:10.1074/jbc.M112.359976
  Sequence
[ath:AT1G14030] [ag:AAA69903]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.259
IUBMB Enzyme Nomenclature: 2.1.1.259
ExPASy - ENZYME nomenclature database: 2.1.1.259
BRENDA, the Enzyme Database: 2.1.1.259

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