A0A2G8Y4J3 · A0A2G8Y4J3_TOXGO

Function

function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.

Miscellaneous

Parasitic protozoa lack the de novo purine biosynthesis pathway and rely exclusively on the salvage pathway for their purine nucleotide requirements.

Caution

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

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.

TypeIDPosition(s)Description
Binding site44-50GTP (UniProtKB | ChEBI)
Active site45Proton acceptor
Binding site45Mg2+ (UniProtKB | ChEBI)
Binding site45-48IMP (UniProtKB | ChEBI)
Binding site70-73IMP (UniProtKB | ChEBI)
Binding site72Mg2+ (UniProtKB | ChEBI)
Binding site72-74GTP (UniProtKB | ChEBI)
Active site73Proton donor
Binding site163IMP (UniProtKB | ChEBI)
Active site174
Binding site177IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site253IMP (UniProtKB | ChEBI)
Binding site268IMP (UniProtKB | ChEBI)
Binding site328-334substrate
Binding site332IMP (UniProtKB | ChEBI)
Binding site334GTP (UniProtKB | ChEBI)
Binding site360-362GTP (UniProtKB | ChEBI)
Binding site446-448GTP (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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylosuccinate synthetase
  • EC number
  • Short names
    AMPSase
    ; AdSS
  • Alternative names
    • IMP--aspartate ligase

Gene names

    • ORF names
      TGCOUG_279450

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • COUG
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Sarcocystidae > Toxoplasma

Accessions

  • Primary accession
    A0A2G8Y4J3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    460
  • Mass (Da)
    50,590
  • Last updated
    2018-01-31 v1
  • Checksum
    D068542238F858E9
MAVSVEGSQDERHLSNCHDIWAERVKQCHGEGSPLVVVVGAQWGDEGKGKLVDILSARADVCARFNGGHNAGHTLEIDGVRYGMHLLPCGIFHTHTIGVIGNGMVIHLKSLLSELEQIQKINPDALNRLLISSRAHLLFDIHQKIDGLQEEAKAKVGDAIGTTRRGIGPCYATKALRSGIRVGELLNFKVFETKYSRLVQELKEQYRLEFDDKEELERHRRYASILAERITDTAAYIRKSVNERKRILVEGANAALLDVDFGTYPYVTSSNTTVGGVCTGLGIPPRFIGLSVGVVKAYTTRVGEGPFPTELTDAIGLHLREKGGEYGTTTGRPRRCGWIDIPALVYTAQINCFDCINLTKLDVLSGLKELKICISYKNKETSAIVAPGEFPCSAEEFSLLEPVYESMAGWNGSLEKCKTLEDLPEAAKAYVRRIEQLLSVQCRWIGVGPGRDDTIEVPAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGQR02001276
EMBL· GenBank· DDBJ
PIM02182.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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