P28650 · PURA1_MOUSE

  • Protein
    Adenylosuccinate synthetase isozyme 1
  • Gene
    Adss1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 committed step in the biosynthesis of AMP from IMP.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Note: Binds 1 Mg2+ ion per subunit.

Activity regulation

Weakly inhibited by AMP non-competitively to all substrates. Inhibited by IMP non-competitively with respect to GTP. Inhibited by fructose 1,6-bisphosphate competitively with respect to IMP.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
12 μMGTP
45 μMIMP
140 μML-aspartate

pH Dependence

Optimum pH is 6.6-6.9.

Pathway

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

Features

Showing features for binding site, active site.

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

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
Molecular Functionadenylosuccinate synthase activity
Molecular FunctionGTP binding
Molecular Functionmagnesium ion binding
Biological Process'de novo' AMP biosynthetic process
Biological ProcessAMP salvage
Biological Processpurine nucleotide 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 like 1
    • Adenylosuccinate synthetase, basic isozyme
    • Adenylosuccinate synthetase, muscle isozyme
      (M-type adenylosuccinate synthetase
      )
    • IMP--aspartate ligase 1

Gene names

    • Name
      Adss1
    • Synonyms
      Adssl1

Organism names

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

Accessions

  • Primary accession
    P28650
  • Secondary accessions
    • Q8CHQ1

Proteomes

Organism-specific databases

Subcellular Location

Membrane ; Peripheral membrane protein
Note: Partially associated with particulate fractions.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000951331-457Adenylosuccinate synthetase isozyme 1

Proteomic databases

PTM databases

Expression

Tissue specificity

High levels in muscle.

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Miscellaneous

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 & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P28650-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    457
  • Mass (Da)
    50,254
  • Last updated
    1996-02-01 v2
  • Checksum
    EBEC85BF907B7FED
MSGTRASNDRPPGTGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIVSRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSARFKNLAHQHQSMFPTLEIDVEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKVLVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGDLLQNRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLSEIKVGISYKLNGKRIPYFPANQEILQKVEVEYETLPGWKADTTGARKWEDLPPQAQSYVRFVENHMGVAVKWVGVGKSRESMIQLF

P28650-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 136-136: L → LENEVPHEPLPSASLLPMCWLLAP

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
J3QN31J3QN31_MOUSEAdss1480

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_008422136in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M74495
EMBL· GenBank· DDBJ
AAA82870.1
EMBL· GenBank· DDBJ
mRNA
BC039943
EMBL· GenBank· DDBJ
AAH39943.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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