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Identification
NameAdenosylhomocysteinase
Synonyms
  • AdoHcyase
  • S-adenosyl-L-homocysteine hydrolase
Gene NameSAH1
Enzyme Class
Biological Properties
General FunctionInvolved in adenosylhomocysteinase activity
Specific FunctionAdenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine
Cellular LocationCytoplasmic
SMPDB Pathways
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
Selenocompound metabolismPW002472 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Selenocompound metabolismec00450 Map00450
SMPDB Reactions
S-Adenosylhomocysteine + waterAdenosine + Homocysteine
KEGG Reactions
S-Adenosylhomocysteine + waterAdenosine + L-Homocysteine
Metabolites
YMDB IDNameView
YMDB00058AdenosineShow
YMDB00198S-AdenosylhomocysteineShow
YMDB00371HomocysteineShow
YMDB00520L-HomocysteineShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
hydrolase activity, acting on ether bonds
trialkylsulfonium hydrolase activity
adenosylhomocysteinase activity
catalytic activity
hydrolase activity
Process
one-carbon metabolic process
metabolic process
cellular metabolic process
Gene Properties
Chromosome Locationchromosome 5
LocusYER043C
Gene Sequence>1350 bp ATGTCTGCTCCAGCTCAAAACTACAAAATCGCTGATATCTCTTTGGCTGCCTTCGGTAGA AAGGAAATCGAATTGGCTGAACATGAAATGCCAGGTTTGATGGCCATCAGAAAGGCTTAC GGTGACGTCCAACCTTTGAAAGGCGCCCGTATTGCTGGTTGTTTGCACATGACCATTCAA ACTGCTGTTTTAATTGAAACTTTAGTTGCTTTGGGTGCCGAAGTTACCTGGTCCTCTTGT AACATCTATTCGACTCAAGATCATGCCGCCGCTGCTATTGCCGCTTCCGGTGTTCCAGTT TTTGCCTGGAAGGGTGAAACTGAAGAAGAGTATTTGTGGTGTATTGAACAACAATTGTTT GCCTTCAAGGACAACAAGAAATTGAACTTGATCTTAGATGATGGTGGTGATTTAACCACT TTAGTTCATGAAAAGCACCCTGAAATGCTGGAAGACTGCTTTGGTCTTTCCGAAGAAACT ACCACCGGTGTTCACCACTTATACAGAATGGTCAAAGAAGGCAAGTTAAAGGTTCCTGCC ATTAACGTTAACGACTCCGTCACTAAGTCCAAGTTTGACAACTTGTACGGCTGTAGAGAA TCCTTAGTCGACGGTATTAAGAGAGCCACTGATGTCATGTTGGCTGGTAAGGTTGCCGTT GTTGCTGGTTACGGTGATGTCGGTAAGGGTTGTGCTGCTGCCTTAAGAGGAATGGGTGCT CGTGTCTTGGTTACCGAAATTGACCCAATCAACGCTTTACAAGCTGCCATGGAAGGCTAC CAAGTTGTTACCATGGAAGATGCATCCCACATTGGTCAAGTTTTCGTTACCACCACTGGT TGTAGAGATATTATCAACGGTGAACATTTCATCAACATGCCAGAAGATGCCATTGTTTGT AACATTGGCCATTTCGATATCGAAATTGATGTCGCCTGGTTAAAGGCTAACGCTAAAGAA TGTATTAACATCAAACCACAAGTCGACCGTTACTTGTTGTCTTCTGGTAGACACGTCATC TTGTTGGCTAACGGTAGATTAGTTAACTTGGGTTGTGCTACTGGTCACTCATCTTTCGTT ATGTCTTGTTCCTTCTCTAACCAAGTCTTAGCTCAAATTGCTTTGTTCAAGTCTAACGAT AAGTCTTTCAGAGAAAAGCACATTGAATTCCAAAAGACAGGCCCATTCGAAGTTGGTGTC CACGTTTTGCCAAAGATCTTGGATGAAGCTGTCGCTAAGTTCCACTTGGGCAACTTGGGT GTTAGATTGACTAAATTGAGTAAAGTCCAATCTGAATACTTGGGTATTCCAGAAGAAGGT CCATTCAAGGCCGACCACTACAGATATTGA
Protein Properties
Pfam Domain Function
Protein Residues449
Protein Molecular Weight49125.10156
Protein Theoretical pI6.2
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Adenosylhomocysteinase MSAPAQNYKIADISLAAFGRKEIELAEHEMPGLMAIRKAYGDVQPLKGARIAGCLHMTIQ TAVLIETLVALGAEVTWSSCNIYSTQDHAAAAIAASGVPVFAWKGETEEEYLWCIEQQLF AFKDNKKLNLILDDGGDLTTLVHEKHPEMLEDCFGLSEETTTGVHHLYRMVKEGKLKVPA INVNDSVTKSKFDNLYGCRESLVDGIKRATDVMLAGKVAVVAGYGDVGKGCAAALRGMGA RVLVTEIDPINALQAAMEGYQVVTMEDASHIGQVFVTTTGCRDIINGEHFINMPEDAIVC NIGHFDIEIDVAWLKANAKECINIKPQVDRYLLSSGRHVILLANGRLVNLGCATGHSSFV MSCSFSNQVLAQIALFKSNDKSFREKHIEFQKTGPFEVGVHVLPKILDEAVAKFHLGNLG VRLTKLSKVQSEYLGIPEEGPFKADHYRY
References
External Links
ResourceLink
Saccharomyces Genome Database SAH1
Uniprot IDP39954
Uniprot NameSAHH_YEAST
GenBank Gene IDAY692801
Genebank Protein ID51013053
General Reference
  • Dietrich, F. S., Mulligan, J., Hennessy, K., Yelton, M. A., Allen, E., Araujo, R., Aviles, E., Berno, A., Brennan, T., Carpenter, J., Chen, E., Cherry, J. M., Chung, E., Duncan, M., Guzman, E., Hartzell, G., Hunicke-Smith, S., Hyman, R. W., Kayser, A., Komp, C., Lashkari, D., Lew, H., Lin, D., Mosedale, D., Davis, R. W., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Nature 387:78-81.9169868
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • 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
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956