A0A927PMX3 · A0A927PMX3_9ACTN

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 site129IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Active site140
Binding site143IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site224IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site239IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site299-305substrate
Binding site303IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site305GTP (UniProtKB | ChEBI)
Binding site331-333GTP (UniProtKB | ChEBI)
Binding site413-415GTP (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
      HT102_13120

Organism names

  • Taxonomic identifier
  • Strain
    • G463
  • Taxonomic lineage
    Bacteria > Bacillati > Actinomycetota > Actinomycetes > Mycobacteriales > Hoyosellaceae > Lolliginicoccus

Accessions

  • Primary accession
    A0A927PMX3

Proteomes

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
    429
  • Mass (Da)
    46,489
  • Last updated
    2023-02-22 v1
  • MD5 Checksum
    345D81F55771D5E836AB95DB8A0D97C2
MPAIVLIGAQWGDEGKGKATDLLGGRVHWVVRYQGGNNAGHTVVLPNGDHFALHLIPSGILTPEVTNVIGNGVVVDPAVLLDELSGLEDRSVDTSRLLISADAHLLMPYHVAIDKVTERFLGNRKIGTTGRGIGPCYQDKIARVGVRAQDVLDESILRRKVEAALEVKNQILTKIYNRRALDADQIVDGVLEQAEGFKHRIADTGLMLGNALDRDEVVLLEGSQGTMLDVDHGTYPFVTSSNPTAGGASVGSGVGPTRITVVLGILKAYTTRVGSGPFPTELFDEQGAYLAKQGGEVGVTTGRARRCGWFDAVIARYATRVNGITDYFLTKLDVLSGLETVPICVGYEIDGKRIDDMPMTQTDIHHAMPVYEEMPGWWEDISEARTFEDLPKTARDYVLRLEELSGAHISCIGVGPGRDQTIVRRDILA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACYWE010000008
EMBL· GenBank· DDBJ
MBD8507424.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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