A0A6P5QZA3 · A0A6P5QZA3_MUSCR

Function

function

Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site42-48GTP (UniProtKB | ChEBI)
Active site43Proton acceptor
Binding site43Mg2+ (UniProtKB | ChEBI)
Binding site43substrate
Binding site43-46IMP (UniProtKB | ChEBI)
Binding site68-71IMP (UniProtKB | ChEBI)
Binding site70Mg2+ (UniProtKB | ChEBI)
Binding site70-72GTP (UniProtKB | ChEBI)
Active site71Proton donor
Binding site163IMP (UniProtKB | ChEBI)
Active site174
Binding site177IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site256IMP (UniProtKB | ChEBI)
Binding site271IMP (UniProtKB | ChEBI)
Binding site331-337substrate
Binding site335IMP (UniProtKB | ChEBI)
Binding site337GTP (UniProtKB | ChEBI)
Binding site363-365GTP (UniProtKB | ChEBI)
Binding site445-448GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenylosuccinate synthase activity
Molecular FunctionGTP binding
Molecular Functionmagnesium ion binding
Biological Process'de novo' AMP biosynthetic process
Biological ProcessIMP metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylosuccinate synthetase isozyme 1
  • EC number
  • Short names
    AMPSase 1
    ; AdSS 1
  • Alternative names
    • Adenylosuccinate synthetase, basic isozyme
    • Adenylosuccinate synthetase, muscle isozyme
      (M-type adenylosuccinate synthetase
      )
    • IMP--aspartate ligase 1

Gene names

    • Name
      Adssl1
    • Synonyms
      ADSS1
      , ADSSL1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    A0A6P5QZA3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-24Disordered

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    457
  • Mass (Da)
    50,254
  • Last updated
    2020-12-02 v1
  • Checksum
    EBEC85BF907B7FED
MSGTRASNDRPPGTGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIVSRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSARFKNLAHQHQSMFPTLEIDVEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKVLVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGDLLQNRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLSEIKVGISYKLNGKRIPYFPANQEILQKVEVEYETLPGWKADTTGARKWEDLPPQAQSYVRFVENHMGVAVKWVGVGKSRESMIQLF

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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