A0AAD1B4E9 · A0AAD1B4E9_9PSED
- ProteinAdenylosuccinate synthetase
- GenepurA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids430 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- GTP + IMP + L-aspartate = GDP + 2 H+ + N6-(1,2-dicarboxyethyl)-AMP + phosphate
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 | 13-19 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 14 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 14 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 14-17 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: DEGK | ||||||
Binding site | 39-42 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: NAGH | ||||||
Binding site | 41 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 41-43 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 42 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 130 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Active site | 141 | |||||
Sequence: K | ||||||
Binding site | 144 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 225 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: Q | ||||||
Binding site | 240 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 300-306 | substrate | ||||
Sequence: ATTGRAR | ||||||
Binding site | 304 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 306 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 332-334 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KLD | ||||||
Binding site | 414-416 | GTP (UniProtKB | ChEBI) | ||||
Sequence: STG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | adenylosuccinate synthase activity | |
Molecular Function | GTP binding | |
Molecular Function | magnesium ion binding | |
Biological Process | purine nucleotide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate synthetase
- EC number
- Short namesAMPSase ; AdSS
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0AAD1B4E9
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length430
- Mass (Da)46,820
- Last updated2024-05-29 v1
- ChecksumEA76C7FCD045B5C6