A0A2M7MH77 · A0A2M7MH77_9BACT

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 site40-43IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site42Mg2+ (UniProtKB | ChEBI)
Binding site42-44GTP (UniProtKB | ChEBI)
Active site43Proton 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 site221IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site236IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site297-303substrate
Binding site301IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site303GTP (UniProtKB | ChEBI)
Binding site329-331GTP (UniProtKB | ChEBI)
Binding site411-413GTP (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
      COZ26_01735

Organism names

Accessions

  • Primary accession
    A0A2M7MH77

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
    423
  • Mass (Da)
    47,133
  • Last updated
    2018-04-25 v1
  • Checksum
    C504EF2794DB9387
MPVRGVVGCQWGDEGKGKIIDLLCALSRIGVVARFQGGANAGHTVVVKSEKYILHLIPSGILHPNVQCYIGNGVVIEPDKLLYEIDLLESKNFQVRNRLAISTNAHVIMPYHIILDKSKESNPNLFIGTTGRGIGPAYVDKVDRIGIRMMDLQSPDLLREKLALNLKLKASHLKRKKVNLDKILQDYLAYGERLQPCLRDVSRLINEDITAGKNILLEGAQGTLLDVDFGTYPYVTSSSPIAGGACTGLGIGPTKIDDVIGVFKAYTTRVGEGPFPTEFLSYFYTERIREWGKEFGATTGRPRRCGWFDGVLARFAARINGLTEMAITKLDVLDRLATVQICTGYHVDGDCCRDLPTDLAIIRDCQPVYEELPGWQQNTTNIREFDKLPKQAQIYLRRIEELVDVPLRLVSVGSERDQTIWCK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PFJV01000040
EMBL· GenBank· DDBJ
PIX92456.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
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