Q9Y0Y2 · PURA_DROME
- ProteinAdenylosuccinate synthetase
- GeneAdss
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids447 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Plays a role in the regulation of adult life span
Plays a role in the regulation of adult life span
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 | 35-41 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 36 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 36 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 36-39 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: DEGK | ||||||
Binding site | 61-64 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: NAGH | ||||||
Binding site | 63 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 63-65 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 64 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 153 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 167 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 245 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 260 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 320-326 | substrate | ||||
Sequence: VTTKRKR | ||||||
Binding site | 324 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 326 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 352-354 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KLD | ||||||
Binding site | 435-437 | 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 lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9Y0Y2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Mutant flies show life span extension and increased activity. Heterozygous mutants show increased ratios of AMP:ATP (3 to 4-fold) and ADP:ATP (2-fold), also observed in response to caloric restriction, and associated with life span extension phenotypes in yeast and worms.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000095136 | 1-447 | Adenylosuccinate synthetase | |||
Sequence: MSASATNGTHYEQLHQGRTKMYKSKVDVVLGAQWGDEGKGKVVDMLASDVDIVCRCQGGNNAGHTVVANGTEFDFHLLPSGVVNEKCVSVIGNGVVIHLPSLFDEVLKNEAKGLQHLENRLIISDRAHLVFDFHQHVDGMQEAEKGGKSLGTTKKGIGPAYSSKATRNGIRVGELLGDFNLFSEKFKSIVATHVRLFPSINVDVEAELARYKDYADKVRPYVKDTICFLHTALRNGKTILVEGANAAMLDIDFGTYPYVTSSNCSIGGVLTGLGLPPQTIGEVIGVVKAYTTRVGDGPFPTEQLNDIGDLLQTRGFEVGVTTKRKRRCGWLDIPLLKYTSLVNGYTCICLTKLDILDTLPEIKVAVAYKKPNGEKLDHFPGTIAELGNIEVEYAVLPGWQTSTEEVRNFKELPENAQSYVRLLESELSVPVRWVGVGKGRESIINVH |
Proteomic databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length447
- Mass (Da)48,901
- Last updated1999-11-01 v1
- Checksum5599F75993FA8701
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 422 | in Ref. 4; AAF55811/AAM29433 | ||||
Sequence: L → F |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014297 EMBL· GenBank· DDBJ | AAF55811.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF145694 EMBL· GenBank· DDBJ | AAD38669.1 EMBL· GenBank· DDBJ | mRNA | ||
AY113428 EMBL· GenBank· DDBJ | AAM29433.1 EMBL· GenBank· DDBJ | mRNA |