A0A0E3GUW0 · A0A0E3GUW0_SACSO
- ProteinAdenylosuccinate lyase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids474 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N6-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.
Catalytic activity
- (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarateThis reaction proceeds in the forward direction.
Pathway
Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity | |
Molecular Function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate lyase
- EC number
- Short namesASL
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Saccharolobus
Accessions
- Primary accessionA0A0E3GUW0
Proteomes
Structure
Family & Domains
Features
Showing features for coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 351-378 | |||||
Sequence: LDSMISLLRNLRVNFENIEKNLNLTKGQ | ||||||
Domain | 376-456 | Adenylosuccinate lyase C-terminal | ||||
Sequence: KGQIMAESLMINLTLKGMKRHEAHQYVNKLTSKVRQTGKTLLEVCLEDSLILSYFSKQELENVLNPKNYLGSYDKLIERAI |
Sequence similarities
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length474
- Mass (Da)53,848
- Last updated2015-06-24 v1
- Checksum0BF91C5516ADCA30
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP011055 EMBL· GenBank· DDBJ | AKA73558.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP011056 EMBL· GenBank· DDBJ | AKA76256.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP011057 EMBL· GenBank· DDBJ | AKA78948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP033235 EMBL· GenBank· DDBJ | AZF68026.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP033236 EMBL· GenBank· DDBJ | AZF70646.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP033237 EMBL· GenBank· DDBJ | AZF73266.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP033238 EMBL· GenBank· DDBJ | AZF75891.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP033239 EMBL· GenBank· DDBJ | AZF78500.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP033240 EMBL· GenBank· DDBJ | AZF81104.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP033241 EMBL· GenBank· DDBJ | AZF83743.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP050869 EMBL· GenBank· DDBJ | QPG50547.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LT549890 EMBL· GenBank· DDBJ | SAI83779.1 EMBL· GenBank· DDBJ | Genomic DNA |