Q8P2U1 · PURA_STRP8

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
    • Ordered locus names
      spyM18_0156

Organism names

Accessions

  • Primary accession
    Q8P2U1

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000952441-430Adenylosuccinate synthetase

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    47,393
  • Last updated
    2002-10-19 v1
  • MD5 Checksum
    5504DF9C6192672BCF2BD1A7DE502E42
MTSVVVVGTQWGDEGKGKITDFLSADAEVIARYQGGDNAGHTIVIDGKKFKLHLIPSGIFFPQKISVIGNGVVVNPKSLVKELAYLHDEGVTTDNLRISDRAHVILPYHIQLDQLQEDAKGDNKIGTTIKGIGPAYMDKAARVGIRIADLLDKDIFAERLRINLAEKNRLFEKMYDSTPLDFDAIFEEYYAYGQEIKQYVTDTSVILNDALDAGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKINKVVGVCKAYTSRVGDGPFPTELFDEVGERIREVGHEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNSIDVLSGLDAVKICVAYDLDGERIDYYPASLEQLKRCKPIYEELPGWQEDITGVRSLDELPENARNYVRRIGELVGVRISTFSVGPGREQTNILESVWASI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE009949
EMBL· GenBank· DDBJ
AAL96963.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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