F0NPQ3 · F0NPQ3_SULIH
- ProteinArgininosuccinate synthase
- GeneargG
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids406 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- ATP + L-aspartate + L-citrulline = 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 | 21-29 | ATP (UniProtKB | ChEBI) | ||||
Sequence: AYSGGLDTT | ||||||
Binding site | 99 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 129 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 131 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 135 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 135 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 136 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 139 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 186 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 195 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 268 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 280 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | argininosuccinate synthase activity | |
Molecular Function | ATP binding | |
Biological Process | arginine biosynthetic process |
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 lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Sulfolobus
Accessions
- Primary accessionF0NPQ3
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-177 | Arginosuccinate synthase-like N-terminal | ||||
Sequence: KIVLAYSGGLDTTVSIRWLKETFKAEVITVTVDVGQKDDFKKIEERAYIAGASKHYTIDVIKEFANNYISYAIKLNGLYEGVYPLSTALARPLIAEKVVEVAKKEKADAVAHGSTSKGNDQVRFDLTVKALYPDVKIIAPARIWSMTREDEIKYAKEKGIP | ||||||
Domain | 185-397 | Arginosuccinate synthase C-terminal | ||||
Sequence: YSIDENLWGRSIEGDIISDPSVEVTEDAFEWTKQIANNKEIISIEFSNGVPTAVDGEQMELHKLIGLLNLKFGNHGFGRVEHIENRVVGFKSREVYEVPAALGLIYSHIDLEKTIYTPTELRFKKYVDQLWSDLVYQGLWFEPLRETLHKIADEMNKWIAGEVRVEVNNGSFRILGRKSDYSPYSEKLASYNKGWYPSDEMARGFIEIWGMHS |
Sequence similarities
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length406
- Mass (Da)46,255
- Last updated2011-05-03 v1
- ChecksumFEAF401F66491672
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002426 EMBL· GenBank· DDBJ | ADX82810.1 EMBL· GenBank· DDBJ | Genomic DNA |