A0A2T5NG08 · A0A2T5NG08_9NEIS

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 site13-19GTP (UniProtKB | ChEBI)
Active site14Proton acceptor
Binding site14Mg2+ (UniProtKB | ChEBI)
Binding site14-17IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site39-42IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site41Mg2+ (UniProtKB | ChEBI)
Binding site41-43GTP (UniProtKB | ChEBI)
Active site42Proton 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 site225IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site240IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site300-306substrate
Binding site304IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site306GTP (UniProtKB | ChEBI)
Binding site332-334GTP (UniProtKB | ChEBI)
Binding site414-416GTP (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
      DB032_05390

Organism names

  • Taxonomic identifier
  • Strain
    • Panama
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Chromobacteriaceae > Chromobacterium

Accessions

  • Primary accession
    A0A2T5NG08

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
    431
  • Mass (Da)
    46,538
  • Last updated
    2018-07-18 v1
  • MD5 Checksum
    DB5647640BEFC7969BF487DEFB30093A
MSKNVVVIGTQWGDEGKGKIVDWLTDHARAVVRFQGGHNAGHTLVVGGKKTVLRLIPSGILRDDVECFIGNGVVLSPEALLKEIDELETAGVNVAARLKISEGCPLILPYHVALDQAREAAKGAGKIGTTGRGIGPCYEDKVARRALKVIDLFDTARFAEKLKENVEYYNFMLTQLFQAEPVSFDVILADTLKLAERIKPMVADVSRTLYDMNQAGIPLLFEGAQGTLLDIDHGTYPYVTSSNCVAGAAAPGAGVAPQMLNYVLGIVKGYTTRVGSGPFPTEQENEIGMFLAKRGNEFGSVTGRPRRCGWFDAAALKRSIQINGVSGLCVTKLDVMDGLEEIKLCVGYTLDGEKVDILPFGSDAVSQCVPVYETMPGWTESTFGAKRWEDLPANAQAYLTRIAEVCGAPVDIISTGPDREETIVMRHPFGL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QARX01000001
EMBL· GenBank· DDBJ
PTU64382.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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