Sequence of METH_ECOLI
EC Number:2.1.1.13
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine
Other sequences found for EC No. 2.1.1.13
General information:
Sequence
0 MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK
60 PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA
120 RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI
180 ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA
240 LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ
300 AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG
360 ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI
420 AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV
480 VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ
540 DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG
600 QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN
660 KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK
720 SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL
780 GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA
840 HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR
900 TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY
960 PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT
1020 HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH
1080 DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP
1140 ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV
1200 EDYARRKGMS VTEVERWLAP NLGYDAD
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
58344
Old I.G.,Margarita D.,Glass R.E.,Saint-Girons I.
Nucleotide sequence of the metH gene of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2.
Gene
87
15-21
1990
58345
Banerjee R.V.,Johnston N.L.,Sobeski J.K.,Datta P.,Matthews R.G.
Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain.
J. Biol. Chem.
264
13888-13895
1989
58346
Drummond J.T.,Loo R.R.,Matthews R.G.
Electrospray mass spectrometric analysis of the domains of a large enzyme: observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase.
Biochemistry
32
9282-9289
1993
58347
Blattner F.R.,Burland V.D.,Plunkett G. III,Sofia H.J.,Daniels D.L.
Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.
Nucleic Acids Res.
21
5408-5417
1993
58348
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
58349
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
58350
Goulding C.W.,Postigo D.,Matthews R.G.
Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine.
Biochemistry
36
8082-8091
1997
58351
Luschinsky C.L.,Drummond J.T.,Matthews R.G.,Ludwig M.L.
Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli.
J. Mol. Biol.
225
557-560
1992
58352
Jarrett J.T.,Amaratunga M.,Drennan C.L.,Scholten J.D.,Sands R.H.,Ludwig M.L.,Matthews R.G.
Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity.
Biochemistry
35
2464-2475
1996
58353
Goulding C.W.,Matthews R.G.
Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation.
Biochemistry
36
15749-15757
1997
58354
VanBogelen R.A.,Abshire K.Z.,Moldover B.,Olson E.R.,Neidhardt F.C.
Escherichia coli proteome analysis using the gene-protein database.
Electrophoresis
18
1243-1251
1997
58355
Peariso K.,Zhou Z.S.,Smith A.E.,Matthews R.G.,Penner-Hahn J.E.
Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy.
Biochemistry
40
987-993
2001
58357
Drennan C.L.,Huang S.,Drummond J.T.,Matthews R.G.,Ludwig M.L.
How a protein binds B12: a 3.0 A X-ray structure of B12-binding domains of methionine synthase.
Science
266
1669-1674
1994
58358
Dixon M.M.,Huang S.,Matthews R.G.,Ludwig M.L.
The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12.
Structure
4
1263-1275
1996
58359
Bandarian V.,Pattridge K.A.,Lennon B.W.,Huddler D.P.,Matthews R.G.,Ludwig M.L.
Domain alternation switches B(12)-dependent methionine synthase to the activation conformation.
Nat. Struct. Biol.
9
53-56
2002
