A0A7Y6D3C3 · A0A7Y6D3C3_9MICC
- ProteinAdenylosuccinate synthetase
- GenepurA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids429 (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
- 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 | 12-18 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 13 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 13 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 13-16 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: DEGK | ||||||
Binding site | 38-41 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: NAGH | ||||||
Binding site | 40 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 40-42 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 41 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 128 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Active site | 139 | |||||
Sequence: K | ||||||
Binding site | 142 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 223 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: Q | ||||||
Binding site | 238 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 298-304 | substrate | ||||
Sequence: VNTGRPR | ||||||
Binding site | 302 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 304 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 330-332 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KLD | ||||||
Binding site | 412-414 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GVG |
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
- EC number
- Short namesAMPSase ; AdSS
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Pseudarthrobacter
Accessions
- Primary accessionA0A7Y6D3C3
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length429
- Mass (Da)46,498
- Last updated2021-06-02 v1
- Checksum7A563F33E7FF830D