A0A2G8Y4J3 · A0A2G8Y4J3_TOXGO
- ProteinAdenylosuccinate synthetase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids460 (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.
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Miscellaneous
Parasitic protozoa lack the de novo purine biosynthesis pathway and rely exclusively on the salvage pathway for their purine nucleotide requirements.
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 | 44-50 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 45 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 45 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 45-48 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DEGK | ||||||
Binding site | 70-73 | IMP (UniProtKB | ChEBI) | ||||
Sequence: NAGH | ||||||
Binding site | 72 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 72-74 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 73 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 163 | IMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 174 | |||||
Sequence: K | ||||||
Binding site | 177 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 253 | IMP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 268 | IMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 328-334 | substrate | ||||
Sequence: TTTGRPR | ||||||
Binding site | 332 | IMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 334 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 360-362 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KLD | ||||||
Binding site | 446-448 | 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 |
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 lineageEukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Sarcocystidae > Toxoplasma
Accessions
- Primary accessionA0A2G8Y4J3
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length460
- Mass (Da)50,590
- Last updated2018-01-31 v1
- ChecksumD068542238F858E9