P52201 · PUR8_SPICI
- ProteinAdenylosuccinate lyase
- GenepurB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- 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
- N6-(1,2-dicarboxyethyl)-AMP = fumarate + AMPThis 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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 4-5 | N6-(1,2-dicarboxyethyl)-AMP (UniProtKB | ChEBI) | |||
Binding site | 67-69 | N6-(1,2-dicarboxyethyl)-AMP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Mycoplasmatota > Mollicutes > Entomoplasmatales > Spiroplasmataceae > Spiroplasma
Accessions
- Primary accessionP52201
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000137883 | 1-88 | Adenylosuccinate lyase | ||
Interaction
Subunit
Homotetramer and homodimer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Family and domain databases
Sequence
- Sequence statusFragment
- Length88
- Mass (Da)10,264
- Last updated1996-10-01 v1
- MD5 Checksum5E284AD97F2A953DB43B2C5E10FABD5B
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 88 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L22971 EMBL· GenBank· DDBJ | AAA26587.1 EMBL· GenBank· DDBJ | Genomic DNA |