S-adenosylmethionine synthase (P0A817)

Identification
Name:S-adenosylmethionine synthase
Synonyms:
  • AdoMet synthase
  • MAT
  • Methionine adenosyltransferase
Gene Name:metK
Enzyme Class:
Biological Properties
General Function:Involved in methionine adenosyltransferase activity
Specific Function:Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. Is essential for growth
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0L-Methionine ↔ 1.0S-Adenosylmethionine + 1.0Phosphate + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Phosphate + 1.0Pyrophosphate + 1.0S-Adenosylmethionine ↔ 1.0Adenosine triphosphate + 1.0L-Methionine + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Pyrophosphate
1.0L-Methionine + 1.0Water + 1.0Adenosine triphosphate → 1.0Phosphate + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0S-adenosyl-L-methionine
1.0L-Methionine + 1.0Water + 1.0Adenosine triphosphate → 1.0Phosphate + 1.0Pyrophosphate + 1.0S-adenosyl-L-methionine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0L-Methionine ↔ 1.0S-Adenosylmethionine + 1.0Phosphate + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00696L-MethionineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB01185S-AdenosylmethionineMetaboCard
ECMDB11118Se-AdenosylselenomethionineMetaboCard
ECMDB03379TriphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
methionine adenosyltransferase activity
nucleoside binding
purine nucleoside binding
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
cellular metabolic process
metabolic process
one-carbon metabolic process
Gene Properties
Blattner:b2942
Gene OrientationClockwise
Centisome Percentage:66.49
Left Sequence End3084728
Right Sequence End3085882
Gene Sequence:
>1155 bp
ATGCTGCTGGTACTGGTGCTGATTGGTCTTAATATGCGACCACTGCTCACCTCCGTCGGG
CCACTGCTACCGCAATTGCGCCAGGCGAGCGGAATGAGCTTTAGCGTGGCTGCCCTGTTG
ACCGCTCTGCCGGTGGTTACCATGGGCGGGCTGGCGCTGGCCGGAAGCTGGCTTCATCAG
CATGTCAGCGAACGTCGCAGTGTCGCCATCAGTCTGTTGCTGATTGCCGTCGGTGCATTG
ATGCGTGAGCTTTACCCGCAAAGTGCGCTGCTGCTTAGCAGCGCACTGCTTGGTGGGGTG
GGGATCGGCATCATTCAGGCGGTGATGCCTTCGGTGATTAAACGGCGGTTTCAGCAGCGC
ACGCCACTGGTGATGGGGCTGTGGTCCGCGGCTCTGATGGGCGGCGGTGGGCTTGGTGCC
GCCATAACGCCCTGGTTAGTTCAACATAGCGAAACCTGGTATCAAACACTCGCCTGGTGG
GCGCTGCCTGCCGTTGTTGCGCTCTTTGCCTGGTGGTGGCAAAGCGCCCGCGAGGTCGCC
TCTTCCCACAAGACAACAACCACTCCGGTTCGCGTGGTATTCACTCCCCGCGCGTGGACG
CTGGGTGTTTACTTCGGTCTGATTAACGGCGGTTACGCCAGCCTGATTGCCTGGTTACCC
GCTTTCTATATTGAGATTGGTGCCAGCGCGCAGTACAGCGGTTCCTTACTGGCATTGATG
ACGCTTGGGCAAGCCGCAGGAGCTTTGCTGATGCCTGCTATGGCTCGCCATCAGGATCGG
CGCAAACTGTTAATGCTGGCGCTGGTGTTACAACTGGTGGGGTTCTGCGGCTTTATCTGG
CTGCCGATGCAATTGCCGGTATTGTGGGCGATGGTGTGTGGGTTAGGTCTGGGCGGCGCG
TTTCCGCTCTGTTTGCTGCTGGCGCTCGATCACTCTGTGCAACCGGCTATTGCTGGCAAG
CTGGTGGCGTTTATGCAGGGAATCGGTTTTATCATCGCCGGGCTTGCCCCGTGGTTTTCT
GGCGTGCTGCGTAGTATCAGCGGCAATTACCTGATGGACTGGGCATTTCATGCGCTGTGC
GTCGTTGGGCTGATGATCATAACCCTGCGTTTTGCACCAGTACGTTTTCCGCAGCTGTGG
GTCAAAGAGGCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:384
Protein Molecular Weight:41951
Protein Theoretical pI:5
PDB File:1RG9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>S-adenosylmethionine synthase
MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTS
AWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQ
GLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVG
IDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDC
GLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVS
YAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGH
FGREHFPWEKTDKAQLLRDAAGLK
References
External Links:
ResourceLink
Uniprot ID:P0A817
Uniprot Name:METK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674483
PDB ID:1RG9
Ecogene ID:EG10589
Ecocyc:EG10589
ColiBase:b2942
Kegg Gene:b2942
EchoBASE ID:EB0584
CCDB:METK_ECOLI
BacMap:16130843
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Fu, Z., Hu, Y., Markham, G. D., Takusagawa, F. (1996). "Flexible loop in the structure of S-adenosylmethionine synthetase crystallized in the tetragonal modification." J Biomol Struct Dyn 13:727-739. Pubmed: 8723769
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Markham, G. D., DeParasis, J., Gatmaitan, J. (1984). "The sequence of metK, the structural gene for S-adenosylmethionine synthetase in Escherichia coli." J Biol Chem 259:14505-14507. Pubmed: 6094561
  • McQueney, M. S., Markham, G. D. (1995). "Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition." J Biol Chem 270:18277-18284. Pubmed: 7629147
  • Moore, R. C., Boyle, S. M. (1990). "Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli." J Bacteriol 172:4631-4640. Pubmed: 2198270
  • Reczkowski, R. S., Markham, G. D. (1995). "Structural and functional roles of cysteine 90 and cysteine 240 in S-adenosylmethionine synthetase." J Biol Chem 270:18484-18490. Pubmed: 7629176
  • Reczkowski, R. S., Taylor, J. C., Markham, G. D. (1998). "The active-site arginine of S-adenosylmethionine synthetase orients the reaction intermediate." Biochemistry 37:13499-13506. Pubmed: 9753435
  • Satishchandran, C., Taylor, J. C., Markham, G. D. (1993). "Isozymes of S-adenosylmethionine synthetase are encoded by tandemly duplicated genes in Escherichia coli." Mol Microbiol 9:835-846. Pubmed: 8231813
  • Takusagawa, F., Kamitori, S., Markham, G. D. (1996). "Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution." Biochemistry 35:2586-2596. Pubmed: 8611562
  • Takusagawa, F., Kamitori, S., Misaki, S., Markham, G. D. (1996). "Crystal structure of S-adenosylmethionine synthetase." J Biol Chem 271:136-147. Pubmed: 8550549
  • Taylor, J. C., Markham, G. D. (1999). "The bifunctional active site of s-adenosylmethionine synthetase. Roles of the active site aspartates." J Biol Chem 274:32909-32914. Pubmed: 10551856
  • Taylor, J. C., Markham, G. D. (2000). "The bifunctional active site of S-adenosylmethionine synthetase. Roles of the basic residues." J Biol Chem 275:4060-4065. Pubmed: 10660564
  • Wei, Y., Newman, E. B. (2002). "Studies on the role of the metK gene product of Escherichia coli K-12." Mol Microbiol 43:1651-1656. Pubmed: 11952912
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842