Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A191HWQ6 · A0A191HWQ6_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.

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 site130IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Active site141
Binding site144IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site226IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site241IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site301-307substrate
Binding site305IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site307GTP (UniProtKB | ChEBI)
Binding site333-335GTP (UniProtKB | ChEBI)
Binding site415-417GTP (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
      AZF37_08630

Organism names

Accessions

  • Primary accession
    A0A191HWQ6

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
    430
  • Mass (Da)
    47,621
  • Last updated
    2016-10-05 v1
  • MD5 Checksum
    D41EA28034CE6C7438E87E379B341777
MSSVVLIGSQWGDEGKGKITDYLAEEAEYVVRYQGGNNAGHTVIVGEEEYKLHLIPSGIIYPGTKCMIGNGVVVDPGVLLEEMEYLKEKGIHVTPDNLKLSLHAHMIMPYHKILDGLEEEKRGAAKIGTTKRGIGPCYVDKIARTGLRFCDLQNKVSFRKILTQNVQAKNEILEKLYNQKELLDLEAIYNEFMAYGEHLLPFIDDVSYILNDALRDNKKVLFEGAQGTLLDIDHGTYPFVTSSNPTAGYAPVGTGVGPTKINCVLGITKAYLTRVGEGPFPTELFDATGKLLSAVGNEVGTTTGRPRRCGWFDGVLMNYATNINGMTHLTITKLDVLDQLPTIKICTAYEIDGVKTTTFPPDLERLSKAKPIYEELPGWQTSTKGIKTFNELPENAKKYLKRIEEFLSVKIALVAVGPKRDEAIELEKLF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP014606
EMBL· GenBank· DDBJ
AMP21212.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help