A0A0W0C789 · A0A0W0C789_CANGB

Function

function

Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all dinucleoside polyphosphates, provided the phosphate chain contains at least 3 phosphates and that 1 of the 2 bases composing the nucleotide is a purine. Is most effective on dinucleoside triphosphates. Negatively regulates intracellular dinucleoside polyphosphate levels, which elevate following heat shock.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site30substrate
Binding site87substrate
Binding site93-96substrate
Active site100Tele-AMP-histidine intermediate
Binding site102substrate
Site117Important for induction of apoptosis

GO annotations

AspectTerm
Molecular Functionbis(5'-adenosyl)-triphosphatase activity
Molecular Functionnucleotide binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bis(5'-adenosyl)-triphosphatase
  • EC number

Gene names

    • ORF names
      AO440_001656

Organism names

Accessions

  • Primary accession
    A0A0W0C789

Proteomes

Organism-specific databases

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain5-117HIT
Motif98-102Histidine triad motif

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    190
  • Mass (Da)
    22,284
  • Last updated
    2016-03-16 v1
  • Checksum
    6123A27F85AD2162
MSGSTPIYFSKFLVTEQVFFRTRFSYALVNLKPITKGHVLVVPLRSQVVQLSQLTPQENADYFNTVQLIHQFMKWVYKAQAVNIAIQDGPEAGQSVPHLHTHIIPRYKENNIGDKVYEHLDEWDLRRDEYMKARDMNEEGTNLRPDQDDVRIARSMEEMKKEVDFLKAQLEEFLSNHCDVKKWLATDARQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LLZZ01000107
EMBL· GenBank· DDBJ
KTB07688.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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