Q7V2H1 · PURA_PROMP

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.

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 site128IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site142IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site223IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site238IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site298-304substrate
Binding site302IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site304GTP (UniProtKB | ChEBI)
Binding site330-332GTP (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
    • Synonyms
      adeK
    • Ordered locus names
      PMM0506

Organism names

Accessions

  • Primary accession
    Q7V2H1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000952121-436Adenylosuccinate synthetase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    436
  • Mass (Da)
    47,868
  • Last updated
    2003-10-01 v1
  • Checksum
    713A503E0FA6E7A8
MANVVVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTIVVDDKVLKLHLIPSGILYRETICLIGSGTVVDPKILLKEIDMLIDNGIDISGLKISSTSHVTMPYHRLLDEAMEADRGSNKIGTTGRGIGPTYADKSQRNGIRIRDLLNEDRLRDVIEIPLKEKNGLLEKIYGIAPLNKDEIIEEYLDYGQRLSKHVVDCTRTIHAAAKNKKNILFEGAQGTLLDLDHGTYPYVTSSNPISGGACIGAGVGPTLIDRVIGVAKAYTTRVGEGPFPTELQGSINDQLCDRGSEFGTTTGRRRRCGWFDGIIGKYAVYVNGLDCLAVTKLDVLDELDEIQVCIAYELDGKEIDYFPTNSDDLKKCKPIFKKLKGWQCSTANCRKLSDLPENAMNYLRFLAELMEVPIAIVSLGANRDQTIVIEDPIHGPKRALLR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX548174
EMBL· GenBank· DDBJ
CAE18965.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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