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Identification
NameS-adenosylmethionine synthase 2
Synonyms
  • AdoMet synthase 2
  • Methionine adenosyltransferase 2
  • MAT 2
Gene NameSAM2
Enzyme Class
Biological Properties
General FunctionCoenzyme transport and metabolism
Specific FunctionCatalyzes the formation of S-adenosylmethionine from methionine and ATP
Cellular LocationNot Available
SMPDB Pathways
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
Selenocompound metabolismPW002472 ThumbThumb?image type=greyscaleThumb?image type=simple
beta-Alanine metabolismPW002381 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Selenocompound metabolismec00450 Map00450
beta-Alanine metabolismec00410 Map00410
SMPDB Reactions
L-Methionine + Adenosine triphosphate + waterphosphate + Pyrophosphate + S-Adenosyl-L-methionine
KEGG Reactions
L-Methionine + Adenosine triphosphate + waterPyrophosphate + phosphate + S-Adenosylmethionine
Metabolites
YMDB IDNameView
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00297S-AdenosylmethionineShow
YMDB00318L-MethionineShow
YMDB00438S-Adenosyl-L-methionineShow
YMDB00890waterShow
YMDB00907phosphateShow
GO Classification
Component
Not Available
Function
methionine adenosyltransferase activity
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
catalytic activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
transferase activity
Process
one-carbon metabolic process
metabolic process
cellular metabolic process
Gene Properties
Chromosome Locationchromosome 4
LocusYDR502C
Gene Sequence>1155 bp ATGTCCAAGAGCAAAACTTTCTTATTTACCTCTGAATCCGTCGGTGAAGGTCACCCAGAC AAGATTTGTGACCAAGTTTCTGATGCTATTTTGGACGCTTGTTTAGAACAAGATCCATTC TCCAAGGTTGCCTGTGAAACAGCTGCCAAAACTGGTATGATTATGGTTTTCGGTGAAATT ACCACCAAAGCTAGACTTGACTACCAACAAATAGTAAGAGATACCATCAAGAAGATTGGT TATGACGATTCTGCCAAGGGTTTCGACTACAAGACATGTAATGTTTTAGTAGCTATCGAA CAACAATCTCCAGATATCGCTCAAGGTCTGCACTATGAAAAGAGCTTAGAAGACTTAGGT GCTGGTGACCAAGGTATAATGTTTGGTTACGCTACAGACGAAACTCCAGAAGGGTTACCA TTGACCATTCTTTTGGCTCACAAATTGAACATGGCTATGGCAGATGCTAGAAGAGATGGT TCTCTCCCATGGTTGAGACCAGACACAAAGACTCAAGTCACTGTCGAATACGAAGACGAC AATGGTAGATGGGTTCCAAAGAGGATAGATACCGTTGTTATTTCTGCTCAACATGCTGAT GAAATTTCCACCGCTGACTTGAGAACTCAACTTCAAAAAGATATTGTTGAAAAGGTCATA CCAAAGGATATGTTAGACGAAAATACCAAATATTTCATCCAACCATCCGGTAGATTCGTC ATCGGTGGTCCTCAAGGTGACGCTGGTTTGACCGGTAGAAAGATTATTGTCGACGCTTAC GGTGGTGCCTCATCCGTCGGTGGTGGTGCCTTCTCCGGTAAGGACTATTCCAAGGTCGAT CGTTCCGCTGCTTACGCTGCTAGATGGGTTGCCAAGTCTCTAGTTGCCGCTGGTTTGTGT AAGAGAGTCCAAGTCCAATTTTCATATGCTATTGGTATTGCTGAACCATTGTCTTTACAT GTGGACACCTATGGTACAGCTACAAAATCAGATGACGAAATCATTGAAATTATTAAGAAG AACTTCGACTTGAGACCAGGTGTGTTAGTAAAGGAATTAGATTTGGCTAGACCAATTTAC TTACCAACCGCTTCTTATGGTCACTTCACTAATCAAGAGTACTCATGGGAAAAACCAAAG AAATTGGAATTTTAA
Protein Properties
Pfam Domain Function
Protein Residues384
Protein Molecular Weight42255.5
Protein Theoretical pI4.98
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>S-adenosylmethionine synthase 2 MSKSKTFLFTSESVGEGHPDKICDQVSDAILDACLEQDPFSKVACETAAKTGMIMVFGEI TTKARLDYQQIVRDTIKKIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGLHYEKSLEDLG AGDQGIMFGYATDETPEGLPLTILLAHKLNMAMADARRDGSLPWLRPDTKTQVTVEYEDD NGRWVPKRIDTVVISAQHADEISTADLRTQLQKDIVEKVIPKDMLDENTKYFIQPSGRFV IGGPQGDAGLTGRKIIVDAYGGASSVGGGAFSGKDYSKVDRSAAYAARWVAKSLVAAGLC KRVQVQFSYAIGIAEPLSLHVDTYGTATKSDDEIIEIIKKNFDLRPGVLVKELDLARPIY LPTASYGHFTNQEYSWEKPKKLEF
References
External Links
ResourceLink
Saccharomyces Genome Database SAM2
Uniprot IDP19358
Uniprot NameMETK2_YEAST
GenBank Gene IDM23368
Genebank Protein ID295659
General Reference
  • Thomas, D., Rothstein, R., Rosenberg, N., Surdin-Kerjan, Y. (1988). "SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes." Mol Cell Biol 8:5132-5139.3072475
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Garrels, J. I., McLaughlin, C. S., Warner, J. R., Futcher, B., Latter, G. I., Kobayashi, R., Schwender, B., Volpe, T., Anderson, D. S., Mesquita-Fuentes, R., Payne, W. E. (1997). "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Electrophoresis 18:1347-1360.9298649
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S. P. (2003). "A proteomics approach to understanding protein ubiquitination." Nat Biotechnol 21:921-926.12872131
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358