M0KGP2 · M0KGP2_9EURY

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 site11-17GTP (UniProtKB | ChEBI)
Active site12Proton acceptor
Binding site12Mg2+ (UniProtKB | ChEBI)
Binding site12-15IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site37-40IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site39Mg2+ (UniProtKB | ChEBI)
Binding site39-41GTP (UniProtKB | ChEBI)
Active site40Proton donor
Binding site127IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Active site138
Binding site141IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site232IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site247IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site326-332substrate
Binding site330IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site332GTP (UniProtKB | ChEBI)
Binding site358-360GTP (UniProtKB | ChEBI)
Binding site443-445GTP (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
      C435_09049

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 33799
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloarculaceae > Haloarcula

Accessions

  • Primary accession
    M0KGP2

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
    458
  • Mass (Da)
    49,390
  • Last updated
    2013-04-03 v1
  • Checksum
    5875E98EC0AFBD79
MTVTIVGSQLGDEGKGGIVDLYGDDVDVVARYQGGDNAGHTVVHEGEEYKLSLVPSGAIRGKVGVLGNGCVVNPRTLFDEIDTLQERGLDPDVRIAERAHVILPFHRVLDGIEEELKSETDDEVGTTGRGIGPTYEDKAGRRGVRVGDLLDPDVLRERLEYVVPQKRAVVEDVYDLDVHELDDPDAFDVDAIFEEFREFGRRFEAEDMTVNAGAFLSATIDEGQNVMLEGAQGTIIDIDHGNYPYVTSSNPTAGGAATGTGLSPGVVGDGEVIGIVKAYLTRVGSGPLPTELGGVVGDTPGYDEQGEGENEELANYIREEGGEYGTVTGRPRRVGWLDLPMLRHSTRVSGFTGIAINHLDVLAGLDEVKVGHTYTLDGEELASMPATTEQWAKCEANFRSFDGWPEVDWADAAEEGYDALPENAKAYVEYIESELDTPAYAIGVGPGRGETIVREQPF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOLS01000044
EMBL· GenBank· DDBJ
EMA19349.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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