Sequence of MMT1_ARATH
EC Number:2.1.1.12
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
S-adenosyl-L-methionine + L-methionine + H+ = S-adenosyl-L-homocysteine + S-methyl-L-methionine
Other sequences found for EC No. 2.1.1.12
General information:
Sequence
0 MADLSSVDEF LNQCKQSGDA AYGALRSVLE RLEDPNTRSK ARIFLSDIYK RVGSSETSLQ
60 TYHFHIQDIY LDQYEGFQSR KKLTMMVIPS IFIPEDWSFT FYEGLNRHPD TIFKDKTVSE
120 LGCGNGWISI AIAAKWLPSK VYGLDINPRA VKISWINLYL NALDDNGEPV YDEEKKTLLD
180 RVEFYESDLL GYCRDNKIQL ERIVGCIPQI LNPNPEAMSK LITENASEEF LHSLSNYCAL
240 QGFVEDQFGL GLIARAVEEG ISVIKPAGIM IFNMGGRPGQ GVCRRLFERR GVRVTQMWQT
300 KILQAADTDI SALVEIERSS PHRFEFFMGL SGDQPICART AWAYGKAGGR ISHALSVYSC
360 QIRQPNLVKI IFDFLKNGFQ EISNSLDLSF EDETVADEKI PFLAYLASVL KNSSYFPFEP
420 PAGSKRFCSL IAGFMRTYHR IPINQDNIVV FPSRAVAIES AFRLFSPRLA IVDEHLTRQL
480 PRSWLTSLAI EDTSMDKSDD QITVIESPHQ SDLMIELIKK LKPQVVVTGM APFEVITSSS
540 FLHLLEVTKE IGCRLFLDIS DHFELSSLPA SNGVLKYLAE NQLPSHAAII CGLVKNKVYS
600 DLEVAFVITE VDAIAKALSK TVEVLEGHTA IISQYYYGCL FHELLAFQLA DRHAPAERES
660 EKAKSEEIIG FSSSAVSILK DAELSVTEID ETSLIHMDVD QSFLQIPQSV KAAIFESFVR
720 QNISEAEVDI NPSIKQFVWS NYGFPTKSST GFVYADGSLA LFNKLVICCA QEGGTLCLPA
780 GTNGNYVAAA KFLKANVVNI PTESSDGFKL TEKTLTKALE SVKKPWVCIS GPTVSPTGLV
840 YSNEEMDILL STCAKFGAKV IIDTSFSGLE YSATSWDLKN ALSKMDSSLS VSLLGCLSLN
900 LLSGAIKLGF LVLDQSLIDA FHTLPGLSKP HSTVKYAAKK MLALKEEKAS DFLDAVSETI
960 KTLEGRSRRL KEVLQNSGWE VIQPSAGISM VAKPKAYLNK KVKLKAGDGQ EIVELTDSNM
1020 RDVFLSHTGV CLNSGSWTGI PGYCRFSFAL EDSEFDKAIE SIAQFKSVLA N
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
697620
Bourgis F.,Roje S.,Nuccio M.L.,Fisher D.B.,Tarczynski M.C.,Li C.,Herschbach C.,Rennenberg H.,Pimenta M.J.,Shen T.-L.,Gage D.A.,Hanson A.D.
S-methylmethionine plays a major role in phloem sulfur transport and is synthesized by a novel type of methyltransferase.
Plant Cell
11
1485-1498
1999
697622
Cheng C.Y.,Krishnakumar V.,Chan A.P.,Thibaud-Nissen F.,Schobel S.,Town C.D.
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.
Plant J.
89
789-804
2017
697623
Yamada K.,Lim J.,Dale J.M.,Chen H.,Shinn P.,Palm C.J.,Southwick A.M.,Wu H.C.,Kim C.J.,Nguyen M.,Pham P.K.,Cheuk R.F.,Karlin-Newmann G.,Liu S.X.,Lam B.,Sakano H.,Wu T.,Yu G.,Miranda M.,Quach H.L.,Tripp M.,Chang C.H.,Lee J.M.,Toriumi M.J.,Chan M.M.,Tang C.C.,Onodera C.S.,Deng J.M.,Akiyama K.,Ansari Y.,Arakawa T.,Banh J.,Banno F.,Bowser L.,Brooks S.Y.,Carninci P.,Chao Q.,Choy N.,Enju A.,Goldsmith A.D.,Gurjal M.,Hansen N.F.,Hayashizaki Y.,Johnson-Hopson C.,Hsuan V.W.,Iida K.,Karnes M.,Khan S.,Koesema E.,Ishida J.,Jiang P.X.,Jones T.,Kawai J.,Kamiya A.,Meyers C.,Nakajima M.,Narusaka M.,Seki M.,Sakurai T.,Satou M.,Tamse R.,Vaysberg M.,Wallender E.K.,Wong C.,Yamamura Y.,Yuan S.,Shinozaki K.,Davis R.W.,Theologis A.,Ecker J.R.
Empirical analysis of transcriptional activity in the Arabidopsis genome.
Science
302
842-846
2003
697624
Tagmount A.,Berken A.,Terry N.
An essential role of s-adenosyl-L-methionine:L-methionine s-methyltransferase in selenium volatilization by plants. Methylation of selenomethionine to selenium-methyl-L-selenium-methionine, the precursor of volatile selenium.
Plant Physiol.
130
847-856
2002
697625
Ranocha P.,McNeil S.D.,Ziemak M.J.,Li C.,Tarczynski M.C.,Hanson A.D.
The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and activity.
Plant J.
25
575-584
2001
697626
Kocsis M.G.,Ranocha P.,Gage D.A.,Simon E.S.,Rhodes D.,Peel G.J.,Mellema S.,Saito K.,Awazuhara M.,Li C.,Meeley R.B.,Tarczynski M.C.,Wagner C.,Hanson A.D.
Insertional inactivation of the methionine s-methyltransferase gene eliminates the s-methylmethionine cycle and increases the methylation ratio.
Plant Physiol.
131
1808-1815
2003
697627
Maor R.,Jones A.,Nuehse T.S.,Studholme D.J.,Peck S.C.,Shirasu K.
Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants.
Mol. Cell. Proteomics
6
601-610
2007
697628
Bienvenut W.V.,Sumpton D.,Martinez A.,Lilla S.,Espagne C.,Meinnel T.,Giglione C.
Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
Mol. Cell. Proteomics
11
0-0
2012
