A0A351Q9A9 · A0A351Q9A9_9SPIR
- ProteinArgininosuccinate synthase
- GeneargG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids454 (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 | 42-50 | ATP (UniProtKB | ChEBI) | ||||
Sequence: AYSGGLDTT | ||||||
Binding site | 120 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 125 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 150 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 152 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 156 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 156 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 157 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 160 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 211 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 220 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 297 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 309 | 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 | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Spirochaetota > Spirochaetia > Spirochaetales > Treponemataceae > Treponema
Accessions
- Primary accessionA0A351Q9A9
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 38-200 | Arginosuccinate synthase-like N-terminal | ||||
Sequence: KVVLAYSGGLDTTVIIPWLKENYDYDVIAVCIDVGQGDDWKAIKSRALKTGASACYVVDARQEYIEEYVWPALKANAIYEDEYLLGTSTARPLIGKILVEYARQEKAVAICHGATGKGNDQVRFELAIKAFAPDLKVIAAWRDPKWNMDSREAEIKYLEDRKL | ||||||
Domain | 210-428 | Arginosuccinate synthase C-terminal | ||||
Sequence: YSRDENIWHLSHEGLELEKTENEPNYKHMLKNTVVPEEAPAAGEYVKIDFEKGIPVAVNGKKMDALKLLLELNKIGGRNGIGLVDICENRCVGMKSRGVYETPGGAILYFAHRMLEHLCLDRDTYHYKQQLSIKVAELIYDGKWFTTLFDACMAFVDKTEETVTGWVKLKLCKGAIRGAGSYSKYSLYNESIASFKTGELYDHKDAQGFITLFGLPLKV |
Sequence similarities
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length454
- Mass (Da)50,821
- Last updated2018-11-07 v1
- Checksum187E21CC3FF152B2