A0A6P5QZA3 · A0A6P5QZA3_MUSCR
- ProteinAdenylosuccinate synthetase isozyme 1
- GeneAdssl1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids457 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
Catalytic activity
- IMP + L-aspartate + GTP = N6-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H+
Cofactor
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 42-48 | GTP (UniProtKB | ChEBI) | |||
Active site | 43 | Proton acceptor | |||
Binding site | 43 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 43 | substrate | |||
Binding site | 43-46 | IMP (UniProtKB | ChEBI) | |||
Binding site | 68-71 | IMP (UniProtKB | ChEBI) | |||
Binding site | 70 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 70-72 | GTP (UniProtKB | ChEBI) | |||
Active site | 71 | Proton donor | |||
Binding site | 163 | IMP (UniProtKB | ChEBI) | |||
Active site | 174 | ||||
Binding site | 177 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 256 | IMP (UniProtKB | ChEBI) | |||
Binding site | 271 | IMP (UniProtKB | ChEBI) | |||
Binding site | 331-337 | substrate | |||
Binding site | 335 | IMP (UniProtKB | ChEBI) | |||
Binding site | 337 | GTP (UniProtKB | ChEBI) | |||
Binding site | 363-365 | GTP (UniProtKB | ChEBI) | |||
Binding site | 445-448 | GTP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | adenylosuccinate synthase activity | |
Molecular Function | GTP binding | |
Molecular Function | magnesium ion binding | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | IMP metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate synthetase isozyme 1
- EC number
- Short namesAMPSase 1 ; AdSS 1
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionA0A6P5QZA3
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length457
- Mass (Da)50,254
- Last updated2020-12-02 v1
- ChecksumEBEC85BF907B7FED