The domain within your query sequence starts at position 402 and ends at position 563; the E-value for the AdoHcyase_NAD domain shown below is 2.21e-103.
S-adenosyl-L-homocysteine hydrolase ( EC 3.3.1.1 ) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. AdoHcyase is an ubiquitous enzyme which binds and requires NAD + as a cofactor. AdoHcyase is a highly conserved protein [ (PUBMED:1631127) ] of about 430 to 470 amino acids.
This entry represents the glycine-rich region in the central part of AdoHcyase, which is thought to be involved in NAD-binding [ (PUBMED:1631127) ].
Family alignment:
There are 17321 AdoHcyase_NAD domains in 17318 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing AdoHcyase_NAD domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with AdoHcyase_NAD domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing AdoHcyase_NAD domain in the selected taxonomic class.
Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteinehydrolase from Rhodobacter capsulatus.
Proc Natl Acad Sci U S A. 1992; 89: 6328-32
Display abstract
The genetic locus ahcY, encoding the enzyme S-adenosyl-L-homocysteinehydrolase (EC 3.3.1.1) from the bacterium Rhodobacter capsulatus, has beenmapped by mutational analysis to within a cluster of genes involved inregulating the induction and maintenance of the bacterial photosyntheticapparatus. Sequence analysis demonstrates that ahcY encodes a 51-kDapolypeptide that displays 64% sequence identity to its human homolog.Insertion mutants in ahcY lack detectable S-adenosyl-L-homocysteinehydrolase activity and, as a consequence, S-adenosyl-L-homocysteineaccumulates in the cells, resulting in a 16-fold decrease in theintracellular ratio of S-adenosyl-L-methionine toS-adenosyl-L-homocysteine as compared to wild-type cells. The ahcYdisrupted strain fails to grow in minimal medium; however, growth isrestored in minimal medium supplemented with methionine or homocysteine orin a complex medium, thereby indicating that the hydrolysis ofS-adenosyl-L-homocysteine plays a key role in the metabolism ofsulfur-containing amino acids. The ahcY mutant, when grown in supplementedmedium, synthesizes significantly reduced levels of bacteriochlorophyll,indicating that modulation of the intracellular ratio ofS-adenosyl-L-methionine to S-adenosyl-L-homocysteine may be an importantfactor in regulating bacteriochlorophyll biosynthesis.