A5KBL5 · A5KBL5_PLAVS
- ProteinAdenylosuccinate lyase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids464 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
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 + fumarate
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 | 13 | AMP (UniProtKB | ChEBI) | |||
Binding site | 14 | AMP (UniProtKB | ChEBI) | |||
Binding site | 86 | AMP (UniProtKB | ChEBI) | |||
Binding site | 87 | AMP (UniProtKB | ChEBI) | |||
Binding site | 88 | AMP (UniProtKB | ChEBI) | |||
Binding site | 122 | AMP (UniProtKB | ChEBI) | |||
Binding site | 280 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 334 | AMP (UniProtKB | ChEBI) | |||
Binding site | 339 | AMP (UniProtKB | ChEBI) | |||
Binding site | 343 | AMP (UniProtKB | ChEBI) | |||
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 | metal ion binding | |
Molecular Function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity | |
Molecular Function | nucleotide binding | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate lyase
- EC number
- Short namesASL
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)
Accessions
- Primary accessionA5KBL5
Proteomes
Organism-specific databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 12-311 | Fumarate lyase N-terminal | |||
Domain | 330-446 | Adenylosuccinate lyase PurB C-terminal | |||
Sequence similarities
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)53,158
- Last updated2007-07-10 v1
- MD5 ChecksumA776C800BECA680702151C87B3E07638
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAKM01000018 EMBL· GenBank· DDBJ | EDL43265.1 EMBL· GenBank· DDBJ | Genomic DNA |