A0A8E9YK14 · A0A8E9YK14_SALET

Function

function

Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.

Catalytic activity

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site12Proton acceptor
Binding site78substrate
Binding site152substrate
Binding site173-174substrate
Active site197Proton donor

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionadenosylhomocysteine nucleosidase activity
Molecular Functionmethylthioadenosine nucleosidase activity
Biological ProcessL-methionine salvage from methylthioadenosine
Biological ProcessL-methionine salvage from S-adenosylmethionine
Biological Processpurine deoxyribonucleoside catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
  • EC number
  • Short names
    MTA/SAH nucleosidase
    ; MTAN
  • Alternative names
    • 5'-deoxyadenosine nucleosidase
      (DOA nucleosidase
      ; dAdo nucleosidase
      )
    • 5'-methylthioadenosine nucleosidase
      (MTA nucleosidase
      )
    • S-adenosylhomocysteine nucleosidase
      (AdoHcy nucleosidase
      ; SAH nucleosidase
      ; SRH nucleosidase
      )

Gene names

    • Name
      mtnN
    • ORF names
      A7S33_019635

Organism names

Accessions

  • Primary accession
    A0A8E9YK14

Subcellular Location

Interaction

Subunit

Homodimer.

Structure

3D structure databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-226Nucleoside phosphorylase

Sequence similarities

Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    232
  • Mass (Da)
    24,472
  • Last updated
    2022-01-19 v1
  • Checksum
    90FFC8E3DB5B9B26
MKIGIIGAMEEEVTLLRDKIDNRQTITLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCIRELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPDAVAVEMEATAIAHVCYNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSTLMVETLVQKLAHG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP075132
EMBL· GenBank· DDBJ
QWJ50563.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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