C3L9T6 · ASSY_BACAC
- ProteinArgininosuccinate synthase
- GeneargG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids401 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 9-17 | ATP (UniProtKB | ChEBI) | ||||
Sequence: AYSGGLDTS | ||||||
Binding site | 86 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 118 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 122 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 122 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 123 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 126 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 174 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 183 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 259 | L-citrulline (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 271 | 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 lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionC3L9T6
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000191878 | 1-401 | Argininosuccinate synthase | |||
Sequence: MEKKKVVLAYSGGLDTSVAIKWLQEKNYDIIALCLDLGEGKDLAFVKEKALSVGAIKSYMIDVQEEFANEYALMAMQAHTLYEGKYPLVSALSRPLIAKKLVEIAEQEGATAVAHGCTGKGNDQVRFEVSIQALNPYLEVIAPVREWKWSREEEIAYAKENNVPIPINLDSPFSIDQNLWGRSNECGILEDPWAAPPEDAYEMTLALEDTPNKPEFVEIGFEAGVPTTLNGTAYPLSELIKTLNALAGKHGVGRIDHVENRLVGIKSREVYECPAAMTLITAHKELEDLTLVKEVAHFKPMIEQKITELIYNGLWFSPLKQALHAFLQETQKNVTGTVRVKLFKGHAIVEGRKSEYSLYDEKLATYTAQDEFNHDAAVGFISLFGLPTKVYSQVNQKKVEA |
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length401
- Mass (Da)44,693
- Last updated2009-06-16 v1
- ChecksumD73DE756DC5AD34E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001215 EMBL· GenBank· DDBJ | ACP12345.1 EMBL· GenBank· DDBJ | Genomic DNA |