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R4YWR3 · R4YWR3_9ACTN

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 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
Active site139
Binding site142IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site224IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site239IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site299-305substrate
Binding site303IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site305GTP (UniProtKB | ChEBI)
Binding site331-333GTP (UniProtKB | ChEBI)
Binding site413-415GTP (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
      BN381_130003

Organism names

Accessions

  • Primary accession
    R4YWR3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    46,812
  • Last updated
    2013-07-24 v1
  • MD5 Checksum
    920DC4DC752324F03EBA8E493BC87A85
MPATIVVGTQWGDEGKGKFTDLFAKEMSMVVRYQGGHNAGHTLVVDGESFALQLVPSGVLYDHIVPVIGNGVVVDPVVLLAEVDMLTAKGVDCSRLRVSGNAHLILPYHQEIDALTERYLGKNKLGTTKRGIGPSYADKSTRVGIRVQDLLDPKIFREKLEAVLEDKNQVLTRVYNRLPFDVDELAETYLGEVRDRMVPYVTDTVGLVHEALEAGQHVLFEGAQATFLDLDHGTYPFVTSSSPTAGGACTGAGVGPRHIDRVVGIAKAYITRVGAGPFPTELFDEVGDHLVDVGHEYGTNTGRRRRPGWFDAVMMRQAVRVNSLSEIALTKLDVLDQLDEVSVCVAYDVDGERHETLPYHQSDLHRATPICETLPGWKTDLTAMTEPGDLPVEARNYLDFLEDQVRCPISLVGVGPGREQFIHRTAS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CANL01000005
EMBL· GenBank· DDBJ
CCM62445.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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