F0V3B1 · F0V3B1_MYCS3
- ProteinAdenylosuccinate synthetase
- GenepurA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids433 (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 | 17-23 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 18 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 18 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 18-21 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: DEGK | ||||||
Binding site | 43-46 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: NAGH | ||||||
Binding site | 45 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 45-47 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 46 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 133 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Active site | 144 | |||||
Sequence: K | ||||||
Binding site | 147 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 227 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: Q | ||||||
Binding site | 242 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 304-310 | substrate | ||||
Sequence: SNTARAR | ||||||
Binding site | 308 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 310 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 336-338 | GTP (UniProtKB | ChEBI) | ||||
Sequence: LVD | ||||||
Binding site | 420-422 | GTP (UniProtKB | ChEBI) | ||||
Sequence: SFG |
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 |
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 > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionF0V3B1
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length433
- Mass (Da)48,759
- Last updated2011-05-03 v1
- Checksum84A40C5F19C77DFE
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FQ790233 EMBL· GenBank· DDBJ | CBZ40333.1 EMBL· GenBank· DDBJ | Genomic DNA |