A0A4D6Y876 · A0A4D6Y876_9GAMM
- ProteinArgininosuccinate synthase
- GeneargG
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids404 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- L-citrulline + L-aspartate + ATP = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H+
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 13-21 | ATP (UniProtKB | ChEBI) | |||
Binding site | 40 | ATP (UniProtKB | ChEBI) | |||
Binding site | 92 | L-citrulline (UniProtKB | ChEBI) | |||
Binding site | 122 | ATP (UniProtKB | ChEBI) | |||
Binding site | 124 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 128 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 128 | L-citrulline (UniProtKB | ChEBI) | |||
Binding site | 129 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 132 | L-citrulline (UniProtKB | ChEBI) | |||
Binding site | 181 | L-citrulline (UniProtKB | ChEBI) | |||
Binding site | 190 | L-citrulline (UniProtKB | ChEBI) | |||
Binding site | 266 | L-citrulline (UniProtKB | ChEBI) | |||
Binding site | 278 | L-citrulline (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | argininosuccinate synthase activity | |
Molecular Function | ATP binding | |
Biological Process | arginine biosynthetic process | |
Biological Process | argininosuccinate metabolic process | |
Biological Process | urea cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArgininosuccinate synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Buchnera
Accessions
- Primary accessionA0A4D6Y876
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 9-170 | Arginosuccinate synthase-like N-terminal | |||
Domain | 180-397 | Arginosuccinate synthase C-terminal | |||
Sequence similarities
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length404
- Mass (Da)45,458
- Last updated2019-07-31 v1
- MD5 Checksum7CFE7E1756E170F46DB363C39B8426EF
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP032999 EMBL· GenBank· DDBJ | QCI25847.1 EMBL· GenBank· DDBJ | Genomic DNA |