A0A4U0ZMT7 · A0A4U0ZMT7_9BACT
- ProteinCarbamoyl phosphate synthase small chain
- GenecarA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids374 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- 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 | 45 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 238 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 240 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 265 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 266 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 269 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 307 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 309 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 310 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Active site | 350 | |||||
Sequence: H | ||||||
Active site | 352 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | carbamoyl-phosphate synthase complex | |
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
Names & Taxonomy
Protein names
- Recommended nameCarbamoyl phosphate synthase small chain
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfobulbia > Desulfobulbales > Desulfocapsaceae > Desulforhopalus
Accessions
- Primary accessionA0A4U0ZMT7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-131 | Carbamoyl-phosphate synthase small subunit N-terminal | ||||
Sequence: MKAIIALEDGTTFEGHSFTGHGEAVGEIVFNTSLSGYQEILTDPSYTGQIVTMTYPLIGNYGTNPEDMESAAAHPKAFLIKEYNSYPSNYRSTKPLAEFLQEYGILGVEGFDTRALVRHIRTKGAMKGIVS | ||||||
Region | 1-189 | CPSase | ||||
Sequence: MKAIIALEDGTTFEGHSFTGHGEAVGEIVFNTSLSGYQEILTDPSYTGQIVTMTYPLIGNYGTNPEDMESAAAHPKAFLIKEYNSYPSNYRSTKPLAEFLQEYGILGVEGFDTRALVRHIRTKGAMKGIVSTRDLDKEALVKKAQEWSGLVGQDMVKKVTCTSPYGWGENEPVAGSNFETAKKPGEKAF |
Sequence similarities
Belongs to the CarA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length374
- Mass (Da)41,024
- Last updated2019-07-31 v1
- Checksum28E8972D1E719476
Keywords
- Technical term