Methionine synthase
Details
- Name
- Methionine synthase
- Synonyms
- 2.1.1.13
- 5-methyltetrahydrofolate--homocysteine methyltransferase
- Methionine synthase, vitamin-B12-dependent
- MS
- Gene Name
- metH
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011146|Methionine synthase MSSKVEQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSK PEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEWTA RTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDGLVAAYRESTKALVEGGADLILI ETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEA LTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQ AGFLNIVGGCCGTTPQHIAAMSRAVEGLAPRKLPEIPVACRLSGLEPLNIGEDSLFVNVG ERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLI AGEPDIARVPIMIDSSKWDVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAV VVMAFDEQGQADTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQ DFIGACEDIKRELPHALISGGVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAG QLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKTDDTANAQQAEWRSWEVN KRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK SARVMKQAVAYLEPFIEASKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDL GVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKA HTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGRKKPR TPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEASIETLRNYIDWTPFFMTWSLAGKY PRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRT HVINVSHHLRQQTEKTGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQH DDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYP ACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQRDQV EDYARRKGMSVTEVERWLAPNLGYDAD
- Number of residues
- 1227
- Molecular Weight
- 135995.81
- Theoretical pI
- 4.71
- GO Classification
- Functionscobalamin binding / methionine synthase activity / protein methyltransferase activity / S-adenosylmethionine-homocysteine S-methyltransferase activity / zinc ion bindingProcesseshomocysteine metabolic process / methionine biosynthetic process / protein methylation / tetrahydrofolate interconversionComponentscytoplasm / cytosol
- General Function
- Zinc ion binding
- Specific Function
- Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011147|Methionine synthase (metH) GTGAGCAGCAAAGTGGAACAACTGCGTGCGCAGTTAAATGAACGTATTCTGGTGCTGGAC GGCGGTATGGGCACCATGATCCAGAGTTATCGACTGAACGAAGCCGATTTTCGTGGTGAA CGCTTTGCCGACTGGCCATGCGACCTCAAAGGCAACAACGACCTGCTGGTACTCAGTAAA CCGGAAGTGATCGCCGCTATCCACAACGCCTACTTTGAAGCGGGCGCGGATATCATCGAA ACCAACACCTTCAACTCCACGACCATTGCGATGGCGGATTACCAGATGGAATCCCTGTCG GCGGAAATCAACTTTGCGGCGGCGAAACTGGCGCGAGCTTGTGCTGACGAGTGGACCGCG CGCACGCCAGAGAAACCGCGCTACGTTGCCGGTGTTCTCGGCCCGACCAACCGCACGGCG TCTATTTCTCCGGACGTCAACGATCCGGCATTTCGTAATATCACTTTTGACGGGCTGGTG GCGGCTTATCGAGAGTCCACCAAAGCGCTGGTGGAAGGTGGCGCGGATCTGATCCTGATT GAAACCGTTTTCGACACCCTTAACGCCAAAGCGGCGGTATTTGCGGTGAAAACGGAGTTT GAAGCGCTGGGCGTTGAGCTGCCGATTATGATCTCCGGCACCATCACCGACGCCTCCGGG CGCACGCTCTCCGGGCAGACCACCGAAGCATTTTACAACTCATTGCGCCACGCCGAAGCT CTGACCTTTGGCCTGAACTGTGCGCTGGGGCCCGATGAACTGCGCCAGTACGTGCAGGAG CTGTCACGGATTGCGGAATGCTACGTCACCGCGCACCCGAACGCCGGGCTACCCAACGCC TTTGGTGAGTACGATCTCGACGCCGACACGATGGCAAAACAGATACGTGAATGGGCGCAA GCGGGTTTTCTCAATATCGTCGGCGGCTGCTGTGGCACCACGCCACAACATATTGCAGCG ATGAGTCGTGCAGTAGAAGGATTAGCGCCGCGCAAACTGCCGGAAATTCCCGTAGCCTGC CGTTTGTCCGGCCTGGAGCCGCTGAACATTGGCGAAGATAGCCTGTTTGTGAACGTGGGT GAACGCACCAACGTCACCGGTTCCGCTAAGTTCAAGCGCCTGATCAAAGAAGAGAAATAC AGCGAGGCGCTGGATGTCGCGCGTCAACAGGTGGAAAACGGCGCGCAGATTATCGATATC AACATGGATGAAGGGATGCTCGATGCCGAAGCGGCGATGGTGCGTTTTCTCAATCTGATT GCCGGTGAACCGGATATCGCTCGCGTGCCGATTATGATCGACTCCTCAAAATGGGACGTC ATTGAAAAAGGTCTGAAGTGTATCCAGGGCAAAGGCATTGTTAACTCTATCTCGATGAAA GAGGGCGTCGATGCCTTTATCCATCACGCGAAATTGTTGCGTCGCTACGGTGCGGCAGTG GTGGTAATGGCCTTTGACGAACAGGGACAGGCCGATACTCGCGCACGGAAAATCGAGATT TGCCGTCGGGCGTACAAAATCCTCACCGAAGAGGTTGGCTTCCCGCCAGAAGATATCATC TTCGACCCAAACATCTTCGCGGTCGCAACTGGCATTGAAGAGCACAACAACTACGCGCAG GACTTTATCGGCGCGTGTGAAGACATCAAACGCGAACTGCCGCACGCGCTGATTTCCGGC GGCGTATCTAACGTTTCTTTCTCGTTCCGTGGCAACGATCCGGTGCGCGAAGCCATTCAC GCAGTGTTCCTCTACTACGCTATTCGCAATGGCATGGATATGGGGATCGTCAACGCCGGG CAACTGGCGATTTACGACGACCTACCCGCTGAACTGCGCGACGCGGTGGAAGATGTGATT CTTAATCGTCGCGACGATGGCACCGAGCGTTTACTGGAGCTTGCCGAGAAATATCGCGGC AGCAAAACCGACGACACCGCCAACGCCCAGCAGGCGGAGTGGCGCTCGTGGGAAGTGAAT AAACGTCTGGAATACTCGCTGGTCAAAGGCATTACCGAGTTTATCGAGCAGGATACCGAA GAAGCCCGCCAGCAGGCTACGCGCCCGATTGAAGTGATTGAAGGCCCGTTGATGGACGGC ATGAATGTGGTCGGCGACCTGTTTGGCGAAGGGAAAATGTTCCTGCCACAGGTGGTCAAA TCGGCGCGCGTCATGAAACAGGCGGTGGCCTACCTCGAACCGTTTATTGAAGCCAGCAAA GAGCAGGGCAAAACCAACGGCAAGATGGTGATCGCCACCGTGAAGGGCGACGTCCACGAC ATCGGTAAAAATATCGTTGGTGTGGTGCTGCAATGTAACAACTACGAAATTGTCGATCTC GGCGTTATGGTGCCTGCGGAAAAAATTCTCCGTACCGCTAAAGAAGTGAATGCTGATCTG ATTGGCCTTTCGGGGCTTATCACGCCGTCGCTGGACGAGATGGTTAACGTGGCGAAAGAG ATGGAGCGTCAGGGCTTCACTATTCCGTTACTGATTGGCGGCGCGACGACCTCAAAAGCG CACACGGCGGTGAAAATCGAGCAGAACTACAGCGGCCCGACGGTGTATGTGCAGAATGCC TCGCGTACCGTTGGTGTGGTGGCGGCGCTGCTTTCCGATACCCAGCGTGATGATTTTGTC GCTCGTACCCGCAAGGAGTACGAAACCGTACGTATTCAGCACGGGCGCAAGAAACCGCGC ACACCACCGGTCACGCTGGAAGCGGCGCGCGATAACGATTTCGCTTTTGACTGGCAGGCT TACACGCCGCCGGTGGCGCACCGTCTCGGCGTGCAGGAAGTCGAAGCCAGCATCGAAACG CTGCGTAATTACATCGACTGGACACCGTTCTTTATGACCTGGTCGCTGGCCGGGAAGTAT CCGCGCATTCTGGAAGATGAAGTGGTGGGCGTTGAGGCGCAGCGGCTGTTTAAAGACGCC AACGACATGCTGGATAAATTAAGCGCCGAGAAAACGCTGAATCCGCGTGGCGTGGTGGGC CTGTTCCCGGCAAACCGTGTGGGCGATGACATTGAAATCTACCGTGACGAAACGCGTACC CATGTGATCAACGTCAGCCACCATCTGCGTCAACAGACCGAAAAAACAGGCTTCGCTAAC TACTGTCTCGCTGACTTCGTTGCGCCGAAGCTTTCTGGTAAAGCAGATTACATCGGCGCA TTTGCCGTGACTGGCGGGCTGGAAGAGGACGCACTGGCTGATGCCTTTGAAGCGCAGCAC GATGATTACAACAAAATCATGGTGAAAGCGCTTGCCGACCGTTTAGCCGAAGCCTTTGCG GAGTATCTCCATGAGCGTGTGCGTAAAGTCTACTGGGGCTATGCGCCGAACGAGAACCTC AGCAACGAAGAGCTGATCCGCGAAAACTACCAGGGCATCCGTCCGGCACCGGGCTATCCG GCCTGCCCGGAACATACGGAAAAAGCCACCATCTGGGAGCTGCTGGAAGTGGAAAAACAC ACTGGCATGAAACTCACAGAATCTTTCGCCATGTGGCCCGGTGCATCGGTTTCGGGTTGG TACTTCAGCCACCCGGACAGCAAGTACTACGCTGTAGCACAAATTCAGCGCGATCAGGTT GAAGATTATGCCCGCCGTAAAGGTATGAGCGTTACCGAAGTTGAGCGCTGGCTGGCACCG AATCTGGGGTATGACGCGGACTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P13009 UniProtKB Entry Name METH_ECOLI GenBank Protein ID 581135 GenBank Gene ID X16584 - General References
- Old IG, Margarita D, Glass RE, Saint Girons I: Nucleotide sequence of the metH gene of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2. Gene. 1990 Mar 1;87(1):15-21. [Article]
- Banerjee RV, Johnston NL, Sobeski JK, Datta P, Matthews RG: 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. 1989 Aug 15;264(23):13888-95. [Article]
- Drummond JT, Loo RR, Matthews RG: 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. 1993 Sep 14;32(36):9282-9. [Article]
- Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Goulding CW, Postigo D, Matthews RG: Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. Biochemistry. 1997 Jul 1;36(26):8082-91. [Article]
- Luschinsky CL, Drummond JT, Matthews RG, Ludwig ML: Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli. J Mol Biol. 1992 May 20;225(2):557-60. [Article]
- Jarrett JT, Amaratunga M, Drennan CL, Scholten JD, Sands RH, Ludwig ML, Matthews RG: Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity. Biochemistry. 1996 Feb 20;35(7):2464-75. [Article]
- Goulding CW, Matthews RG: Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation. Biochemistry. 1997 Dec 16;36(50):15749-57. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Peariso K, Zhou ZS, Smith AE, Matthews RG, Penner-Hahn JE: Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy. Biochemistry. 2001 Jan 30;40(4):987-93. [Article]
- Matthews RG: Cobalamin-dependent methyltransferases. Acc Chem Res. 2001 Aug;34(8):681-9. [Article]
- Drennan CL, Huang S, Drummond JT, Matthews RG, Lidwig ML: How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase. Science. 1994 Dec 9;266(5191):1669-74. [Article]
- Dixon MM, Huang S, Matthews RG, Ludwig M: The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12. Structure. 1996 Nov 15;4(11):1263-75. [Article]
- Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML: Domain alternation switches B(12)-dependent methionine synthase to the activation conformation. Nat Struct Biol. 2002 Jan;9(1):53-6. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details