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Identification
YMDB IDYMDB00198
NameS-Adenosylhomocysteine
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionS-Adenosyl-L-homocysteine (SAH) is an amino acid derivative used in several metabolic pathways in most organisms. It is an intermediate in the synthesis of cysteine and adenosine. SAH is formed by the demethylation of S-adenosyl-L-methionine [Wikipedia]
Structure
Thumb
Synonyms
  • (S)-5'-(S)-(3-Amino-3-carboxypropyl)-5'-thioadenosine
  • 2-S-adenosyl-L-homocysteine
  • 5'-Deoxy-S-adenosyl-L-homocysteine
  • 5'-S-(3-amino-3-carboxypropyl)-5'-thio-L-Adenosine
  • Adenosyl-homo-CYS
  • Adenosyl-L-homocysteine
  • Adenosylhomo-CYS
  • Adenosylhomocysteine
  • Adohcy
  • Formycinylhomocysteine
  • L-5'-S-(3-amino-3-carboxypropyl)-5'-thior-Adenosine
  • L-S-adenosyl-Homocysteine
  • L-S-Adenosylhomocysteine
  • S-(5'-adenosyl)-L-homocysteine
  • S-(5'-deoxyadenosin-5'-yl)-L-homocysteine
  • S-(5'-Deoxyadenosine-5')-L-homocysteine
  • S-adenosyl-homocysteine
  • S-Adenosyl-L-homocysteine
  • SAH
  • (2S)-2-Amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulfanyl)butanoic acid
  • S-[1-(Adenin-9-yl)-1,5-dideoxy-beta-D-ribofuranos-5-yl]-L-homocysteine
  • (2S)-2-Amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulfanyl)butanoate
  • (2S)-2-Amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulphanyl)butanoate
  • (2S)-2-Amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulphanyl)butanoic acid
  • S-[1-(Adenin-9-yl)-1,5-dideoxy-b-D-ribofuranos-5-yl]-L-homocysteine
  • S-[1-(Adenin-9-yl)-1,5-dideoxy-β-D-ribofuranos-5-yl]-L-homocysteine
  • Adenosylhomocysteine, S
  • S Adenosylhomocysteine
CAS number979-92-0
WeightAverage: 384.411
Monoisotopic: 384.12158847
InChI KeyZJUKTBDSGOFHSH-WFMPWKQPSA-N
InChIInChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
IUPAC Name(2S)-2-amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}sulfanyl)butanoic acid
Traditional IUPAC NameS-adenosyl-L-homocysteine
Chemical FormulaC14H20N6O5S
SMILES[H]OC(=O)[C@@]([H])(N([H])[H])C([H])([H])C([H])([H])SC([H])([H])[C@@]1([H])O[C@@]([H])(N2C([H])=NC3=C2N=C([H])N=C3N([H])[H])[C@]([H])(O[H])[C@]1([H])O[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as 5'-deoxy-5'-thionucleosides. These are 5'-deoxyribonucleosides in which the ribose is thio-substituted at the 5'position by a S-alkyl group.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
Class5'-deoxyribonucleosides
Sub Class5'-deoxy-5'-thionucleosides
Direct Parent5'-deoxy-5'-thionucleosides
Alternative Parents
Substituents
  • 5'-deoxy-5'-thionucleoside
  • N-glycosyl compound
  • Glycosyl compound
  • 6-aminopurine
  • Alpha-amino acid
  • Alpha-amino acid or derivatives
  • Pentose monosaccharide
  • L-alpha-amino acid
  • Imidazopyrimidine
  • Purine
  • Hydroxy fatty acid
  • Aminopyrimidine
  • Thia fatty acid
  • Pyrimidine
  • Fatty acyl
  • Monosaccharide
  • Imidolactam
  • N-substituted imidazole
  • Tetrahydrofuran
  • Imidazole
  • Azole
  • Heteroaromatic compound
  • Secondary alcohol
  • Amino acid or derivatives
  • Amino acid
  • 1,2-diol
  • Oxacycle
  • Azacycle
  • Carboxylic acid derivative
  • Carboxylic acid
  • Organoheterocyclic compound
  • Dialkylthioether
  • Sulfenyl compound
  • Thioether
  • Monocarboxylic acid or derivatives
  • Organic oxide
  • Organopnictogen compound
  • Alcohol
  • Carbonyl group
  • Organic oxygen compound
  • Amine
  • Hydrocarbon derivative
  • Organic nitrogen compound
  • Primary amine
  • Primary aliphatic amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point209-211 °C
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility4.08 g/LALOGPS
logP-2.4ALOGPS
logP-4ChemAxon
logS-2ALOGPS
pKa (Strongest Acidic)1.81ChemAxon
pKa (Strongest Basic)9.5ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count10ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area182.63 ŲChemAxon
Rotatable Bond Count7ChemAxon
Refractivity92.72 m³·mol⁻¹ChemAxon
Polarizability38.41 ųChemAxon
Number of Rings3ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • mitochondrion
  • endoplasmic reticulum
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Cholesterol biosynthesis and metabolism CE(10:0)PW002545 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(12:0)PW002548 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(14:0)PW002544 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(16:0)PW002550 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(18:0)PW002551 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Steroid biosynthesisec00100 Map00100
SMPDB Reactions
S-Adenosylhomocysteine + waterAdenosine + Homocysteine
S-Adenosyl-L-methionine + 3-Hexaprenyl-4,5-dihydroxybenzoic acidS-Adenosylhomocysteine + 3-Hexaprenyl-4-hydroxy-5-methoxybenzoic acid
2-Hexaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + S-Adenosyl-L-methionineUbiquinone 6 + S-Adenosylhomocysteine
2-Hexaprenyl-6-methoxy-1,4-benzoquinone + S-Adenosyl-L-methionine2-hexaprenyl-6-methoxy-3-methyl-1,4-benzoquinone + S-Adenosylhomocysteine
zymosterol + S-Adenosyl-L-methionine24-methylidene-5alpha-cholest-8-en-3beta-ol + S-Adenosylhomocysteine + hydron
KEGG Reactions
2-Hexaprenyl-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine2-hexaprenyl-6-methoxy-3-methyl-1,4-benzoquinone + S-Adenosylhomocysteine + hydron
3-Isopropylmalate + S-AdenosylmethionineS-Adenosylhomocysteine + 3-hydroxy-2-isopropyl-4-methoxy-4-oxobutanoate
S-Adenosylhomocysteine + waterAdenosine + L-Homocysteine
zymosterol + oxygen + S-Adenosylmethioninewater + S-Adenosylhomocysteine + hydron + ergosta-5,7,22,24(28)-tetraen-3beta-ol
2-(3-Carboxy-3-aminopropyl)-L-histidine + S-AdenosylmethionineS-Adenosylhomocysteine + hydron + 2-(3-Carboxy-3-(methylammonio)propyl)-L-histidine
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Thomas, D., Becker, A., Surdin-Kerjan, Y. (2000). "Reverse methionine biosynthesis from S-adenosylmethionine in eukaryotic cells." J Biol Chem 275:40718-40724.11013242
  • Mattheakis, L. C., Shen, W. H., Collier, R. J. (1992). "DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae." Mol Cell Biol 12:4026-4037.1508200
  • Tehlivets, O., Hasslacher, M., Kohlwein, S. D. (2004). "S-adenosyl-L-homocysteine hydrolase in yeast: key enzyme of methylation metabolism and coordinated regulation with phospholipid synthesis." FEBS Lett 577:501-506.15556636
  • Gary, J. D., Lin, W. J., Yang, M. C., Herschman, H. R., Clarke, S. (1996). "The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae." J Biol Chem 271:12585-12594.8647869
  • Kodaki, T., Yamashita, S. (1987). "Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes." J Biol Chem 262:15428-15435.2445736
  • Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., Sinclair, D. A. (2003). "Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae." Nature 423:181-185.12736687
  • Katz, J. E., Dumlao, D. S., Wasserman, J. I., Lansdown, M. G., Jung, M. E., Faull, K. F., Clarke, S. (2004). "3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase." Biochemistry 43:5976-5986.15147181
  • Marbois, B., Gin, P., Faull, K. F., Poon, W. W., Lee, P. T., Strahan, J., Shepherd, J. N., Clarke, C. F. (2005). "Coq3 and Coq4 define a polypeptide complex in yeast mitochondria for the biosynthesis of coenzyme Q." J Biol Chem 280:20231-20238.15792955
  • Yamashita, S., Nikawa, J. (1997). "Phosphatidylserine synthase from yeast." Biochim Biophys Acta 1348:228-235.9370337
  • Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). "Growth control of the eukaryote cell: a systems biology study in yeast." J Biol 6:4.17439666
Synthesis Reference:Holy, Antonin; Rosenberg, Ivan. Studies on S-adenosyl-L-homocysteine hydrolase. Part XV. An improved synthesis of S-adenosyl-L-homocysteine and related compounds. Collection of Czechoslovak Chemical Communications (1985), 50(7), 1514-18.
External Links:
ResourceLink
CHEBI ID16680
HMDB IDHMDB00939
Pubchem Compound ID439155
Kegg IDC00021
ChemSpider ID23217251
FOODB IDFDB031150
WikipediaS-adenosyl_homocysteine
BioCyc IDADENOSYL-HOMO-CYS

Enzymes

General function:
Involved in methyltransferase activity
Specific function:
Required for the methylation step in diphthamide biosynthesis
Gene Name:
DPH5
Uniprot ID:
P32469
Molecular weight:
33847.0
Reactions
3 S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine → 3 S-adenosyl-L-homocysteine + 2-(3-carboxy-3-(trimethylammonio)propyl)-L-histidine.
General function:
Involved in methyltransferase activity
Specific function:
Siroheme synthase involved in methionine biosynthesis
Gene Name:
MET1
Uniprot ID:
P36150
Molecular weight:
66124.70313
Reactions
S-adenosyl-L-methionine + uroporphyrinogen III → S-adenosyl-L-homocysteine + precorrin-1.
S-adenosyl-L-methionine + precorrin-1 → S-adenosyl-L-homocysteine + precorrin-2.
General function:
Involved in methyltransferase activity
Specific function:
Non-specific O-methyltransferase that catalyzes the 2 O- methylation steps in the ubiquinone biosynthetic pathway
Gene Name:
COQ3
Uniprot ID:
P27680
Molecular weight:
36330.60156
Reactions
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate → S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate.
S-adenosyl-L-methionine + 3-demethylubiquinone-n → S-adenosyl-L-homocysteine + ubiquinone-n.
S-adenosyl-L-methionine + 2-hexaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinol → S-adenosyl-L-homocysteine + ubiquinol.
General function:
Involved in adenosylhomocysteinase activity
Specific function:
Adenosylhomocysteine 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
Gene Name:
SAH1
Uniprot ID:
P39954
Molecular weight:
49125.10156
Reactions
S-adenosyl-L-homocysteine + H(2)O → L-homocysteine + adenosine.
General function:
Involved in methyltransferase activity
Specific function:
Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation
Gene Name:
TMT1
Uniprot ID:
P32643
Molecular weight:
34768.0
Reactions
S-adenosyl-L-methionine + trans-aconitate → S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate.
General function:
Involved in ubiquinone biosynthetic process
Specific function:
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of COQ3, COQ4, COQ6, COQ7 and COQ9 polypeptides
Gene Name:
COQ4
Uniprot ID:
O13525
Molecular weight:
38626.80078
General function:
Involved in methyltransferase activity
Specific function:
Converts DDMQH2 into DMQH2
Gene Name:
COQ5
Uniprot ID:
P49017
Molecular weight:
34684.19922
Reactions
S-adenosyl-L-methionine + 2-polyprenyl-6-methoxy-1,4-benzoquinol → S-adenosyl-L-homocysteine + 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol.
General function:
Involved in methyltransferase activity
Specific function:
tRNA (uracil-O(2)-)-methyltransferase, which catalyzes the formation of O(2)-methyluracil at position 44 (m2U44) in tRNA(Ser)
Gene Name:
TRM44
Uniprot ID:
Q02648
Molecular weight:
64854.60156
Reactions
S-adenosyl-L-methionine + uridine(44) in tRNA → S-adenosyl-L-homocysteine + 2'-O-methyluridine(44) in tRNA.
General function:
Involved in [cytochrome c]-lysine N-methyltransferase a
Specific function:
Methyltransferase which mediates trimethylation of Lys- 77 of cytochrome c (CYC1)
Gene Name:
CTM1
Uniprot ID:
P38818
Molecular weight:
68283.60156
Reactions
S-adenosyl-L-methionine + [cytochrome c]-L-lysine → S-adenosyl-L-homocysteine + [cytochrome c]-N(6)-methyl-L-lysine.
General function:
Involved in methyltransferase activity
Specific function:
N6-methyltransferase that methylates adenosine residues of some mRNAs and is essential to activate sporulation. N6- methyladenosine (m6A), which is present at internal sites of some mRNAs, is probably required to initiate sporulation. Positive regulator for IME2
Gene Name:
IME4
Uniprot ID:
P41833
Molecular weight:
69395.39844
Reactions
S-adenosyl-L-methionine + m(7)G(5')pppAm → S-adenosyl-L-homocysteine + m(7)G(5')pppm(6)Am.
General function:
Involved in methyltransferase activity
Specific function:
Catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs
Gene Name:
TRM10
Uniprot ID:
Q12400
Molecular weight:
34520.19922
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(1)-methylguanine.
General function:
Involved in tRNA (adenine-N1-)-methyltransferase activity
Specific function:
Catalytic subunit of tRNA (adenine-N(1)-)- methyltransferase, which catalyzes the formation of N(1)- methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency
Gene Name:
GCD14
Uniprot ID:
P46959
Molecular weight:
43919.30078
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(1)-methyladenine.
General function:
Involved in RNA binding
Specific function:
Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs
Gene Name:
TRM1
Uniprot ID:
P15565
Molecular weight:
64051.80078
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(2)-methylguanine.
General function:
Involved in RNA binding
Specific function:
Methylates cytosine to m5C at several positions in different tRNAs and pre-tRNAs containing intron. Able to modify tRNAs at all four positions (34, 40, 48 and 49) at which m5C has been found in tRNAs. May be involved in ribosome biogenesis as its disruption leads to increased sensitivity to the antibiotic paromomycin
Gene Name:
NCL1
Uniprot ID:
P38205
Molecular weight:
77878.0
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine.
General function:
Involved in protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity
Specific function:
Mediates C-terminal methylation of the isoprenylated C- terminal cysteine in A-factor mating pheromone and Ras proteins
Gene Name:
STE14
Uniprot ID:
P32584
Molecular weight:
27887.40039
Reactions
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine → S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester.
General function:
Involved in methyltransferase activity
Specific function:
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop
Gene Name:
TRM7
Uniprot ID:
P38238
Molecular weight:
34700.19922
Reactions
S-adenosyl-L-methionine + rRNA → S-adenosyl-L-homocysteine + rRNA containing 2'-O-methyluridine.
General function:
Involved in protein methyltransferase activity
Specific function:
Methylates arginines in a variety of RNA-binding proteins. Methylates NOP3. Can catalyze both the mono- and asymmetric dimethylation
Gene Name:
HMT1
Uniprot ID:
P38074
Molecular weight:
39785.80078
Reactions
General function:
Involved in methyltransferase activity
Specific function:
Catalyzes the two serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylates the m3G cap on TLC1 telomerase which affects telomere silencing and telomere length regulation. Required for pre-mRNA splicing, pre-rRNA processing and small ribosomal subunit synthesis. Involved in nucleolar structural organization
Gene Name:
TGS1
Uniprot ID:
Q12052
Molecular weight:
36526.80078
Reactions
S-adenosyl-L-methionine + m(7)G(5')pppR-RNA → S-adenosyl-L-homocysteine + m(2,7)G(5')pppR-RNA.
S-adenosyl-L-methionine + m(2,7)G(5')pppR-RNA → S-adenosyl-L-homocysteine + m(2,2,7)G(5')pppR-RNA.
General function:
Involved in RNA binding
Specific function:
Specifically methylates guanosine-18 in various tRNAs
Gene Name:
TRM3
Uniprot ID:
Q07527
Molecular weight:
165046.0
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanosine.
General function:
Involved in methyltransferase activity
Specific function:
Specifically methylates guanosine-4 in various tRNAs with a Gly(CCG), His or Pro signature
Gene Name:
TRM13
Uniprot ID:
Q12383
Molecular weight:
54094.5
Reactions
S-adenosyl-L-methionine + rRNA → S-adenosyl-L-homocysteine + rRNA containing 2'-O-methyluridine.
General function:
Involved in methyltransferase activity
Specific function:
Involved in the control of the cell cycle at the G2/M (mitosis) transition. Cooperates with HSL1 to hyperphosphorylate SWE1, thereby targeting SWE1 for polyubiquitination and subsequent degradation. Acts as a negative regulator of the filamentous growth-signaling pathway through inhibition of STE20
Gene Name:
HSL7
Uniprot ID:
P38274
Molecular weight:
95152.5
Reactions
S-adenosyl-L-methionine + arginine-[histone] → S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
General function:
Involved in methyltransferase activity
Specific function:
Specifically methylates the uridine in position 2791 of mitochondrial 21S rRNA in the fully assembled mitochondrial large ribosomal subunit
Gene Name:
MRM2
Uniprot ID:
P53123
Molecular weight:
37423.10156
Reactions
S-adenosyl-L-methionine + uridine(2791)-2'-O in 21S rRNA → S-adenosyl-L-homocysteine + 2'-O-methyluridine(2791)-2'-O in 21S rRNA.
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S- methylmethionine (SMM) to methionine
Gene Name:
MHT1
Uniprot ID:
Q12525
Molecular weight:
36714.5
Reactions
S-methyl-L-methionine + L-homocysteine → 2 L-methionine.
General function:
Involved in tRNA (guanine-N7-)-methyltransferase activity
Specific function:
Methyltransferase that catalyzes the formation of N(7)- methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity
Gene Name:
TRM8
Uniprot ID:
Q12009
Molecular weight:
33391.19922
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(7)-methylguanine.
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S- methylmethionine (SMM) to methionine
Gene Name:
SAM4
Uniprot ID:
Q08985
Molecular weight:
36668.19922
Reactions
S-methyl-L-methionine + L-homocysteine → 2 L-methionine.
General function:
Involved in nicotinamide N-methyltransferase activity
Specific function:
Putative nicotinamide N-methyltransferase involved in rDNA silencing and in lifespan determination
Gene Name:
NNT1
Uniprot ID:
Q05874
Molecular weight:
29632.30078
Reactions
S-adenosyl-L-methionine + nicotinamide → S-adenosyl-L-homocysteine + 1-methylnicotinamide.
General function:
Involved in phosphatidylethanolamine N-methyltransferas
Specific function:
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
Gene Name:
PEM1
Uniprot ID:
P05374
Molecular weight:
101203.0
Reactions
S-adenosyl-L-methionine + phosphatidylethanolamine → S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.
General function:
Involved in identical protein binding
Specific function:
Specifically methylates guanosine-37 in various tRNAs. Not dependent on the nature of the nucleoside 5' of the target nucleoside
Gene Name:
TRM5
Uniprot ID:
P38793
Molecular weight:
56514.0
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(1)-methylguanine.
General function:
Involved in N-methyltransferase activity
Specific function:
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid methylene fatty acid
Gene Name:
OPI3
Uniprot ID:
P05375
Molecular weight:
23150.09961
Reactions
S-adenosyl-L-methionine + phospholipid olefinic fatty acid → S-adenosyl-L-homocysteine + phospholipid methylene fatty acid.
General function:
Involved in methyltransferase activity
Specific function:
Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation
Gene Name:
SPB1
Uniprot ID:
P25582
Molecular weight:
96484.0
Reactions
S-adenosyl-L-methionine + rRNA → S-adenosyl-L-homocysteine + rRNA containing 2'-O-methylguanosine.
S-adenosyl-L-methionine + rRNA → S-adenosyl-L-homocysteine + rRNA containing 2'-O-methyluridine.
General function:
Involved in methyltransferase activity
Specific function:
Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol
Gene Name:
ERG6
Uniprot ID:
P25087
Molecular weight:
43430.5
Reactions
S-adenosyl-L-methionine + 5-alpha-cholesta-8,24-dien-3-beta-ol → S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3-beta-ol.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2- thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base
Gene Name:
SLM3
Uniprot ID:
Q12093
Molecular weight:
47048.80078
Reactions
S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridylate → S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
General function:
Involved in RNA methyltransferase activity
Specific function:
Catalyzes the formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNA. May also have a role in tRNA stabilization or maturation
Gene Name:
TRM2
Uniprot ID:
P33753
Molecular weight:
72851.79688
Reactions
S-adenosyl-L-methionine + tRNA containing uridine at position 54 → S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54.