M0KGP2 · M0KGP2_9EURY
- ProteinAdenylosuccinate synthetase
- GenepurA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids458 (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 | 11-17 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGG | ||||||
Active site | 12 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 12 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 12-15 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: DEGK | ||||||
Binding site | 37-40 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: NAGH | ||||||
Binding site | 39 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 39-41 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 40 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 127 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Active site | 138 | |||||
Sequence: K | ||||||
Binding site | 141 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 232 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: Q | ||||||
Binding site | 247 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 326-332 | substrate | ||||
Sequence: TVTGRPR | ||||||
Binding site | 330 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 332 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 358-360 | GTP (UniProtKB | ChEBI) | ||||
Sequence: HLD | ||||||
Binding site | 443-445 | 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
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloarculaceae > Haloarcula
Accessions
- Primary accessionM0KGP2
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length458
- Mass (Da)49,390
- Last updated2013-04-03 v1
- Checksum5875E98EC0AFBD79
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOLS01000044 EMBL· GenBank· DDBJ | EMA19349.1 EMBL· GenBank· DDBJ | Genomic DNA |