A0A255ZA77 · A0A255ZA77_9FLAO

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.

TypeIDPosition(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 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
      CHX27_04820
      , CHX27_15005

Organism names

  • Taxonomic identifier
  • Strain
    • TH167
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Flavobacterium

Accessions

  • Primary accession
    A0A255ZA77

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
    423
  • Mass (Da)
    46,876
  • Last updated
    2017-12-20 v1
  • Checksum
    6D10AE7535B4A746
MSVDLLLGLQWGDEGKGKIVDVLTQKYDIIARFQGGPNAGHTLEFDGIKHVLRTIPSGIFHKNAVNIIGNGVVIDPVVFVKELEGLEQFKIDIYNKLIISRKAHLILPTHRLLDAASEASKGKAKIGSTLKGIGPTYMDKTGRNGLRIGDLELDDFKERYRNLADKHEAMIKFYDVSIQYNLAEMENEFFEAIETLKKLQFIDSEAYLFQALKDGKSILAEGAQGSLLDVDFGTYPFVTSSNTTAAGACTGLGIAPNKIKDVYGIFKAYTTRVGSGPFPTELFDEVGETMARIGNEFGSVTGRKRRCGWLDLVALKYAVEINGVTQLMMMKGDVLSGFEELKVCTAYKYRGEIIDHLPYNIEEENVSPVYKSFKGWHADLTGLTEYSDLPTELKDYVSFIEAEVGVPIKIISVGPDRTQTISR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NOXX01000228
EMBL· GenBank· DDBJ
OYQ38463.1
EMBL· GenBank· DDBJ
Genomic DNA
NOXX01000168
EMBL· GenBank· DDBJ
OYQ46162.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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