A0A6B2BZ34 · A0A6B2BZ34_UNCNO
- ProteinArgininosuccinate synthase
- GeneargG
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids395 (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 | 7-15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: AYSGGLDTT | ||||||
Binding site | 85 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 90 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 115 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 117 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 121 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 121 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 122 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 125 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 172 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 181 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 257 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 269 | 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
- Strain
- Taxonomic lineageArchaea > Nitrososphaerota
Accessions
- Primary accessionA0A6B2BZ34
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-163 | Arginosuccinate synthase-like N-terminal | ||||
Sequence: KTVLAYSGGLDTTTSIAWIKEKYGNEVITVTVDVGQQEDFKEIEERAYKAGATKHYFVDAKDEFANEYISMAIKANAMYEKKYPLSTSLARPLIAKKVAEIAKIENADSVAHGSTGKGNDQVRFDVTLRALYPGVKIIAPVREWNMSRDEELKYLLNKGIP | ||||||
Domain | 171-389 | Arginosuccinate synthase C-terminal | ||||
Sequence: FSVDENLWGRSIESGRLEDPYFEPPEEAFAWTVSPEKAPDKPEYIEIGFKKGVPESLNGEKMKLSDMIKIINKTAGRHGVGRIDHIEDRVVGIKSREVYETPAALVLIEAHQEIEKLTLPKTVLRFKPYIEEQWSSMIYDGLWADPLRNALEAFINETQKNVEGEVRLKLFKGSVRVVGRKSEKSLYKHELSTYSSASTFDQKQALGFINLFALQTLVY |
Sequence similarities
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length395
- Mass (Da)44,737
- Last updated2020-06-17 v1
- Checksum41778666750486EF