A0A832S9P8 · A0A832S9P8_9EURY
- Protein5'-deoxyadenosine deaminase
- GenedadD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids462 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Miscellaneous
SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.
Catalytic activity
- 5'-deoxyadenosine + H+ + H2O = 5'-deoxyinosine + NH4+
Cofactor
Note: Binds 1 zinc ion per subunit.
Pathway
Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 63 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 65 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 92 | substrate | ||||
Sequence: E | ||||||
Binding site | 184 | substrate | ||||
Sequence: H | ||||||
Binding site | 211 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 214 | substrate | ||||
Sequence: E | ||||||
Binding site | 329 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 329 | substrate | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 5'-deoxyadenosine deaminase activity | |
Molecular Function | adenosine deaminase activity | |
Molecular Function | metal ion binding | |
Biological Process | S-adenosylmethionine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5'-deoxyadenosine deaminase
- EC number
- Short names5'-dA deaminase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina
Accessions
- Primary accessionA0A832S9P8
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 54-303 | Amidohydrolase-related | ||||
Sequence: VVMPGLVNTHTHAAMTLFRGYADDLQLAEWLENHIWPAEAQLTAEDVYKGSLLACLEMIRSGTTSFADMYFFMDETAKAVEASGIRASLSHGLIELWNEEKGETDLKEGKRFVRAWQGAANGRIKTMYGPHAPNTCSDEFLAKVKEEARKDGAGLHIHVLETEAELLAMKERYGKCSVHMLDDIGFFGPDVLAAHCVWLSDGDIEVLREKGVNVSHNPVSNMKLASGIAPIHKMLERGVNVSLGTDGCAX | ||||||
Domain | 308-431 | Amidohydrolase 3 | ||||
Sequence: ASGTAPVYKMLERGVNVSLGTDGCASNNNLDLFEEMKTAALLHKVSTCNPTALPARQVLEMATVNGAKALGTETGMLKTGMKADLIIVDMKKPHLTPCFDIPSHLVYSAKGSDVRTTIVDGKIL |
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length462
- Mass (Da)50,203
- Last updated2021-09-29 v1
- Checksum84C483B0AB536C1A