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D4S3C5 · D4S3C5_9FIRM

Function

function

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

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.

Type
IDPosition(s)Description
Binding site12-18GTP (UniProtKB | ChEBI)
Active site13Proton acceptor
Binding site13Mg2+ (UniProtKB | ChEBI)
Binding site13-16IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site38-41IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site40Mg2+ (UniProtKB | ChEBI)
Binding site40-42GTP (UniProtKB | ChEBI)
Active site41Proton donor
Binding site128IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site142IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site223IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site238IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site298-304substrate
Binding site302IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site304GTP (UniProtKB | ChEBI)
Binding site330-332GTP (UniProtKB | ChEBI)
Binding site412-414GTP (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

    • Name
      purA
    • ORF names
      HMPREF7545_0040

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 43541
  • Taxonomic lineage
    Bacteria > Bacillota > Negativicutes > Selenomonadales > Selenomonadaceae > Selenomonas

Accessions

  • Primary accession
    D4S3C5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    428
  • Mass (Da)
    46,434
  • Last updated
    2010-06-15 v1
  • MD5 Checksum
    ECD1B51130AC20014D3CB3D42B8730EF
MSTIVITGTQWGDEGKGKIVDYLASQADTVVRYQGGCNAGHTVVAAGEEYKLRLLPSGILYKGTHNIIANGVAFDPKVCLQEMDAMAARGIDTSNIRISDRAHVVMPYHRLMDGIGDAARGADKIGTTGHGIGPCYMDRDNRIGIRVCDLMDGEEFAKKLKKNLESKNKELVSVYDHAPLVYEEVLQEYQGYAARLRPLVTDTIPLVNEEIAAGRKVLFEGAQATMLDIDYGTYPYVTASHPISGGVTIGAGVAPKKIDKVIGVVKAYCTRVGEGPFPTEQLNAIGEKMREAGHEFGTVTGRPRRTGWLDAVVVRHAGLLSGIDYMAVTRLDILDDFDEIKICTGYKHKGELLKGVPASLNVLAEVEPVYETFPGWKTDTSGIRTYDALPAGARKYLERMAEVTGIALGIVSVGPSREQTIVLANDLF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACKT01000003
EMBL· GenBank· DDBJ
EFF67260.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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