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Sequence of METE_THEMA

EC Number:2.1.1.14

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase
Q9X112
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
734
85571
Reaction
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
Other sequences found for EC No. 2.1.1.14

General information:

Sequence
show sequence in fasta format
  0 MKAYAFGFPK IGEKREFKKA LEDFWKGKIT EEQFEEEMNK LRMYMVENYR KNVDVIPSNE
 60 LSYYDFVLDT AVMVGAVPER FGEYRGLSTY FDMARGGKAL EMTKFFNTNY HYLVPEIETE
120 EFYLLENKPL EDYLFFKSKG IETAPWVIGP FTFLYLSKRN GEWIRRPNQM EKLLESLVSV
180 YKEVFEKLVE NGCKEILVNE PAFVCDLEKA HWDLILNVYR ELSEFPLTVF TYYDSVSDYE
240 ACVSLPVKRL HFDFVSNEEN LKNLEKHGFP EDKKLVAGVI NGRQPWKVDL RKVASLVEKL
300 GASAISNSCP LFHLPVTLEL ENNLPGGLKE KLAFAKEKLE ELKMLKDFLE GKTFDLPNVS
360 FEDFAVDLQA VERVRNLPED SFRREKEYTE RDRIQRERLN LPLFPTTTIG SFPQTPEVRK
420 MRSKYRKGEI SKEEYEAFIK EQIKKAIELQ EEIGLDVLVH GEFERTDMVE FFAEKLNGIA
480 TTQNGWVLSY GSRCYRPPII YGTVTRPEPM TLKEITYAQS LTEKPVKGML TGPVTIMSWS
540 YYREDIPERE IAYQIALAIN EEVKDLEEAG IKIVQIDEPA FREKAPIKKS KWPEYFEWAI
600 NAFNLAANAR PETQIHAHMC YSDFNEIIEY IHQLEFDVIS IEASRSKGEI ISAFENFKGW
660 IKQIGVGVWD IHSPAVPSIN EMREIVERVL RVLPKELIWI NPDCGLKTRN WDEVIPSLRN
720 MVALAKEMRE KFES
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
696287
Nelson K.E.,Clayton R.A.,Gill S.R.,Gwinn M.L.,Dodson R.J.,Haft D.H.,Hickey E.K.,Peterson J.D.,Nelson W.C.,Ketchum K.A.,McDonald L.A.,Utterback T.R.,Malek J.A.,Linher K.D.,Garrett M.M.,Stewart A.M.,Cotton M.D.,Pratt M.S.,Phillips C.A.,Richardson D.L.,Heidelberg J.F.,Sutton G.G.,Fleischmann R.D.,Eisen J.A.,White O.,Salzberg S.L.,Smith H.O.,Venter J.C.,Fraser C.M.
Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima.
Nature
399
323-329
1999
696288
Pejchal R.,Ludwig M.L.
Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication.
PLoS Biol.
3
0-0
2005
696289
Koutmos M.,Pejchal R.,Bomer T.M.,Matthews R.G.,Smith J.L.,Ludwig M.L.
Metal active site elasticity linked to activation of homocysteine in methionine synthases.
Proc. Natl. Acad. Sci. U.S.A.
105
3286-3291
2008