P28650 · PURA1_MOUSE
- ProteinAdenylosuccinate synthetase isozyme 1
- GeneAdss1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids457 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. 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.
Activity regulation
Weakly inhibited by AMP non-competitively to all substrates. Inhibited by IMP non-competitively with respect to GTP. Inhibited by fructose 1,6-bisphosphate competitively with respect to IMP.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
12 μM | GTP | |||||
45 μM | IMP | |||||
140 μM | L-aspartate |
pH Dependence
Optimum pH is 6.6-6.9.
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 | 42-48 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 43 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 43 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 43 | substrate | ||||
Sequence: D | ||||||
Binding site | 43-46 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: DEGK | ||||||
Binding site | 68-71 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: NAGH | ||||||
Binding site | 70 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 70-72 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 71 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 163 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 177 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 256 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 271 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 331-337 | substrate | ||||
Sequence: VTTGRKR | ||||||
Binding site | 335 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 337 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 363-365 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KLD | ||||||
Binding site | 445-448 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GVGK |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | adenylosuccinate synthase activity | |
Molecular Function | GTP binding | |
Molecular Function | magnesium ion binding | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | AMP salvage | |
Biological Process | purine nucleotide metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate synthetase isozyme 1
- EC number
- Short namesAMPSase 1 ; AdSS 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP28650
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000095133 | 1-457 | Adenylosuccinate synthetase isozyme 1 | |||
Sequence: MSGTRASNDRPPGTGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIVSRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSARFKNLAHQHQSMFPTLEIDVEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKVLVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGDLLQNRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLSEIKVGISYKLNGKRIPYFPANQEILQKVEVEYETLPGWKADTTGARKWEDLPPQAQSYVRFVENHMGVAVKWVGVGKSRESMIQLF |
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MSGTRASNDRPPGTGGVKRGRLQQ |
Sequence similarities
Belongs to the adenylosuccinate synthetase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P28650-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length457
- Mass (Da)50,254
- Last updated1996-02-01 v2
- ChecksumEBEC85BF907B7FED
P28650-2
- Name2
- Differences from canonical
- 136-136: L → LENEVPHEPLPSASLLPMCWLLAP
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3QN31 | J3QN31_MOUSE | Adss1 | 480 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008422 | 136 | in isoform 2 | |||
Sequence: L → LENEVPHEPLPSASLLPMCWLLAP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M74495 EMBL· GenBank· DDBJ | AAA82870.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039943 EMBL· GenBank· DDBJ | AAH39943.1 EMBL· GenBank· DDBJ | mRNA |