O60060 · CARA_SCHPO
- ProteinCarbamoyl phosphate synthase arginine-specific small chain
- Genearg5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids415 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Small subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, the first step of the arginine biosynthetic pathway (Ref.3). The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia (By similarity).
Miscellaneous
In S.pombe, this enzyme is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control. One is linked to the arginine pathway and is designated CPSase A (arg5-arg4), it is localized to mitochondria and repressed by arginine. A second one, CPSase P, is part of a multifunctional protein (ura1) encoding 3 enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase); it is localized to the cytoplasm and feedback inhibited and repressed by pyrimidines. The carbamoyl phosphate synthesized by each synthase is channeled to its respective pathway, in contrast to Saccharomyces cerevisiae, in which the 2 synthases are localized to the cytoplasm and appear to contribute to the formation of a single cellular pool of carbamoyl phosphate.
Catalytic activity
- hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+
Carbamoyl phosphate synthase arginine-specific small chain
L-glutamine + H2O = L-glutamate + NH4+
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 88 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 272 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 274 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 301 | Nucleophile | |||
Binding site | 302 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 305 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 343 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 345 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 346 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 385 | ||||
Active site | 387 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | carbamoyl-phosphate synthase complex | |
Cellular Component | cytoplasm | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | glutaminase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | arginine biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | urea cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarbamoyl phosphate synthase arginine-specific small chain
- EC number
- Short namesCPS-A
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionO60060
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-17 | Mitochondrion | |||
Chain | PRO_0000290599 | 18-415 | Carbamoyl phosphate synthase arginine-specific small chain | ||
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 225-412 | Glutamine amidotransferase type-1 | |||
Sequence similarities
Belongs to the CarA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length415
- Mass (Da)45,662
- Last updated1998-08-01 v1
- Checksum9D3AF94026943980
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329671 EMBL· GenBank· DDBJ | CAA18888.1 EMBL· GenBank· DDBJ | Genomic DNA |