Q2YM22 · CARA_BRUA2
- ProteinCarbamoyl phosphate synthase small chain
- GenecarA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids407 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia.
Catalytic activity
- 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H+ + L-glutamate + phosphate
Carbamoyl phosphate synthase small chain
H2O + L-glutamine = L-glutamate + NH4+
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 60 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 257 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 259 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 286 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 287 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 290 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 328 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 330 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 331 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Active site | 370 | |||||
Sequence: H | ||||||
Active site | 372 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
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 | 'de novo' UMP biosynthetic process | |
Biological Process | arginine biosynthetic process | |
Biological Process | glutamine metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCarbamoyl phosphate synthase small chain
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionQ2YM22
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000138853 | 1-407 | Carbamoyl phosphate synthase small chain | |||
Sequence: MTETTPKTAPWTVQKRTAVLVLADGTVIEGKGLGATGAVEAEVVFNTALTGYEEILTDPSYAGQIVTFTFPHIGNVGANAEDIEDLTPANRHGAVGAIFKADITAPSNFRAAKDLDSWLKHRGIIALAGIDTRALTALIRERGAQNAVIAHDPNGNFDLDALKARAANWCGLENLDLAKDVTIGQSLVWKELPWTLQDGYGEQDAPQYHVVALDFGVKRNILRLLTGLGAKVTVLPATATAEDVLAHNPDGVFLSNGPGDPAATGEYAVPTIGKLVETGIPLFGICLGHQMLALALGGRTEKMHQGHHGANHPVKDYTTGKVEIVSMNHGFAVDSDSLPENVEETHVSLFDGTNCGLRVVGKPVFSVQHHPEASPGPQDSHYLFRRFINLIRERKGQAPLPEREQAA |
Interaction
Subunit
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-205 | CPSase | ||||
Sequence: MTETTPKTAPWTVQKRTAVLVLADGTVIEGKGLGATGAVEAEVVFNTALTGYEEILTDPSYAGQIVTFTFPHIGNVGANAEDIEDLTPANRHGAVGAIFKADITAPSNFRAAKDLDSWLKHRGIIALAGIDTRALTALIRERGAQNAVIAHDPNGNFDLDALKARAANWCGLENLDLAKDVTIGQSLVWKELPWTLQDGYGEQDA | ||||||
Domain | 209-397 | Glutamine amidotransferase type-1 | ||||
Sequence: HVVALDFGVKRNILRLLTGLGAKVTVLPATATAEDVLAHNPDGVFLSNGPGDPAATGEYAVPTIGKLVETGIPLFGICLGHQMLALALGGRTEKMHQGHHGANHPVKDYTTGKVEIVSMNHGFAVDSDSLPENVEETHVSLFDGTNCGLRVVGKPVFSVQHHPEASPGPQDSHYLFRRFINLIRERKGQ |
Sequence similarities
Belongs to the CarA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length407
- Mass (Da)43,536
- Last updated2006-02-07 v1
- ChecksumD6C01AFF0592F7E2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM040264 EMBL· GenBank· DDBJ | CAJ11458.1 EMBL· GenBank· DDBJ | Genomic DNA |