Methionine synthase

Details

Name
Methionine synthase
Kind
protein
Synonyms
  • 2.1.1.13
  • 5-methyltetrahydrofolate--homocysteine methyltransferase
  • Methionine synthase, vitamin-B12-dependent
  • MS
Gene Name
metH
UniProtKB Entry
P13009Swiss-Prot
Organism
Escherichia coli (strain K12)
NCBI Taxonomy ID
83333
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
Functions
cobalamin binding / methionine synthase activity / protein methyltransferase activity / S-adenosylmethionine-homocysteine S-methyltransferase activity / zinc ion binding
Processes
homocysteine metabolic process / methionine biosynthetic process / protein methylation / tetrahydrofolate interconversion
Components
cytoplasm / cytosol
General 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.
Specific Function
cobalamin binding
Pfam Domain Function
Signal Regions
Not Available
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
ResourceLink
UniProtKB IDP13009
UniProtKB Entry NameMETH_ECOLI
GenBank Protein ID581135
GenBank Gene IDX16584
PDB ID(s)1BMT, 1K7Y, 1K98, 1MSK, 3BUL, 3IV9, 3IVA
KEGG IDecj:JW3979
NCBI Gene ID948522
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. Matthews RG: Cobalamin-dependent methyltransferases. Acc Chem Res. 2001 Aug;34(8):681-9. [Article]
  14. 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]
  15. 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]
  16. 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]

Associated Data

Drug Relations
Not Available