A0BD92 · PURA_PARTE

  • Protein
    Adenylosuccinate synthetase
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).

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.

143150100150200250300350400
TypeIDPosition(s)Description
Binding site21-27GTP (UniProtKB | ChEBI)
Active site22Proton acceptor
Binding site22Mg2+ (UniProtKB | ChEBI)
Binding site22-25IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site47-50IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site49Mg2+ (UniProtKB | ChEBI)
Binding site49-51GTP (UniProtKB | ChEBI)
Active site50Proton donor
Binding site138IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site152IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site230IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site245IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site305-311substrate
Binding site309IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site311GTP (UniProtKB | ChEBI)
Binding site337-339GTP (UniProtKB | ChEBI)
Binding site419-421GTP (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
  • EC number
  • Short names
    AMPSase
    ; AdSS
  • Alternative names
    • IMP--aspartate ligase

Gene names

    • ORF names
      GSPATT00004603001

Organism names

  • Taxonomic identifier
  • Strain
    • Stock d4-2
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Ciliophora > Intramacronucleata > Oligohymenophorea > Peniculida > Parameciidae > Paramecium

Accessions

  • Primary accession
    A0BD92

Proteomes

    • Identifier
    • Component
      Partially assembled WGS sequence

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003992901-431Adenylosuccinate synthetase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    47,560
  • Last updated
    2006-11-28 v1
  • Checksum
    047B9D8B14AA1A3B
MSKCVNGLRSRLTAIIGAQWGDEGKGKLVDILAEKYDYCARFNGGANAGHTIVVGGVKYAFHLLPCGILYQTCMNVIGNGVVVNIPTLFEELAQLDKNRVDYTGRLVISNRAHLVVDGLLEADAKSESDSRKKFLGTTKRGIGPTYSAKALRQGLRVGDLLHWDTFLLKYHSLNAKLREQEGIQIDTQKEINTLKDYRDILINRNMIVDTISLIANARKDGRRILAEGANATMLDIDYGTYPYVTSSSTNVGGVCTGLGVPPSAIETVIGIVKAYTTRVGEGPFPTELTNETGKYLQKTGHEFGATTGRPRRCGWLDIPILRYSIQINGHSSINLTKLDILTGLEEIKIGVNYLLNGKVIDYIPAQLEELAQVEVEYITVKGWKQDISDCKTFSELPVEAQNYIKKIEELLGIPVSWIGNGPQREKIILKD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CT867986
EMBL· GenBank· DDBJ
CAK56509.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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