Sequence of RBCMT_PEA
EC Number:2.1.1.259
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
Other sequences found for EC No. 2.1.1.259
General information:
Sequence
0 MATIFSGGSV SPFLFHTNKG TSFTPKAPIL HLKRSFSAKS VASVGTEPSL SPAVQTFWKW
60 LQEEGVITAK TPVKASVVTE GLGLVALKDI SRNDVILQVP KRLWINPDAV AASEIGRVCS
120 ELKPWLSVIL FLIRERSRED SVWKHYFGIL PQETDSTIYW SEEELQELQG SQLLKTTVSV
180 KEYVKNECLK LEQEIILPNK RLFPDPVTLD DFFWAFGILR SRAFSRLRNE NLVVVPMADL
240 INHSAGVTTE DHAYEVKGAA GLFSWDYLFS LKSPLSVKAG EQVYIQYDLN KSNAELALDY
300 GFIEPNENRH AYTLTLEISE SDPFFDDKLD VAESNGFAQT AYFDIFYNRT LPPGLLPYLR
360 LVALGGTDAF LLESLFRDTI WGHLELSVSR DNEELLCKAV REACKSALAG YHTTIEQDRE
420 LKEGNLDSRL AIAVGIREGE KMVLQQIDGI FEQKELELDQ LEYYQERRLK DLGLCGENGD
480 ILGDLGKFF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1238410
Klein R.R.,Houtz R.L.
Cloning and developmental expression of pea ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase.
Plant Mol. Biol.
27
249-261
1995
1238411
Trievel R.C.,Beach B.M.,Dirk L.M.,Houtz R.L.,Hurley J.H.
Structure and catalytic mechanism of a SET domain protein methyltransferase.
Cell
111
91-103
2002
1238412
Trievel R.C.,Flynn E.M.,Houtz R.L.,Hurley J.H.
Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT.
Nat. Struct. Biol.
10
545-552
2003
1238413
Couture J.F.,Hauk G.,Thompson M.J.,Blackburn G.M.,Trievel R.C.
Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases.
J. Biol. Chem.
281
19280-19287
2006
1238414
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
