A0A125RA36 · A0A125RA36_9EURY

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site64Zn2+ (UniProtKB | ChEBI)
Binding site66Zn2+ (UniProtKB | ChEBI)
Binding site93substrate
Binding site185substrate
Binding site212Zn2+ (UniProtKB | ChEBI)
Binding site215substrate
Binding site300Zn2+ (UniProtKB | ChEBI)
Binding site300substrate

GO annotations

AspectTerm
Molecular Function2'-deoxyadenosine deaminase activity
Molecular Function5'-deoxyadenosine deaminase activity
Molecular Function5'-methylthioadenosine deaminase activity
Molecular Functionadenosine deaminase activity
Molecular Functionmetal ion binding
Molecular FunctionS-adenosylhomocysteine deaminase activity
Biological ProcessS-adenosylmethionine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5'-deoxyadenosine deaminase
  • EC number
  • Short names
    5'-dA deaminase
  • Alternative names
    • 5'-methylthioadenosine deaminase
      (MTA deaminase
      ) (EC:3.5.4.31
      ) . EC:3.5.4.31 (UniProtKB | ENZYME | Rhea)
    • Adenosine deaminase
      (EC:3.5.4.4
      ) . EC:3.5.4.4 (UniProtKB | ENZYME | Rhea)
    • S-adenosylhomocysteine deaminase
      (SAH deaminase
      ) (EC:3.5.4.28
      ) . EC:3.5.4.28 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      dadD
    • ORF names
      TL18_00110

Organism names

  • Taxonomic identifier
  • Strain
    • YE315
  • Taxonomic lineage
    Archaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanobrevibacter

Accessions

  • Primary accession
    A0A125RA36

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain55-405Amidohydrolase-related

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    434
  • Mass (Da)
    47,708
  • Last updated
    2016-04-13 v1
  • Checksum
    5D303AF3B8168C05
MSDNTILIKNALILSPNENFEGKKSLLIKDDIISEISDEIDEGNADKIIDADGKILLPGFVNTHTHLSMTLFRGLADDLSLDSWLNDHIWPMEANLNGDYCYIGALLGAVELIKSGTTTFSDMYFYMEDVARAVDEAGIRAVLSYGMIDFGDEVKRENEIRENLTLFKNCNGMADGRIKVFFGPHSPYTASEELLVKVRELADEYNMGIHIHVSETQKEINDKLEEMGLRPFEYLDKIGLLGPDVVAAHCVWLSDNEIEIIKRNNVKVSHNPCSNMKLASGIAPISKLIENDICVSIGTDGASSNNNLDLIEELKTASLLQKVSTLDPKVLNSDESIAMGTINGAEALGLENEIGSIEVGKKADIILIDTNSANMVPDSSSLSSNIIYSANGSNVDTTICNGKILMENKKLTVLDEEEIYNKARQAIKELKEAI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010834
EMBL· GenBank· DDBJ
AMD16576.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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