A0A0X1TL20 · A0A0X1TL20_9FIRM
- ProteinAdenylosuccinate synthetase
- GenepurA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids426 (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 | 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 | 222 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: Q | ||||||
Binding site | 237 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 297-303 | substrate | ||||
Sequence: TVTGRPR | ||||||
Binding site | 301 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 303 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 329-331 | GTP (UniProtKB | ChEBI) | ||||
Sequence: LLD | ||||||
Binding site | 411-413 | GTP (UniProtKB | ChEBI) | ||||
Sequence: SVG |
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 > Bacillota > Erysipelotrichia > Erysipelotrichales > Turicibacteraceae > Turicibacter
Accessions
- Primary accessionA0A0X1TL20
Proteomes
Subcellular Location
Interaction
Structure
Sequence
- Sequence statusComplete
- Length426
- Mass (Da)47,221
- Last updated2016-04-13 v1
- Checksum56574117FADFF91A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP013476 EMBL· GenBank· DDBJ | AMC08560.1 EMBL· GenBank· DDBJ | Genomic DNA |