A0A9D1A9V7 · A0A9D1A9V7_9FIRM
- ProteinAspartate carbamoyltransferase
- GenepyrB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids306 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway.
Catalytic activity
- carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H+
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 51 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 52 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 80 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 101 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 129 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 132 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 162 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 225 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 264 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 265 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | amino acid metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate carbamoyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillati > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Lachnospiraceae incertae sedis > Candidatus Choladousia
Accessions
- Primary accessionA0A9D1A9V7
Proteomes
Interaction
Subunit
Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 2-141 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | |||
Domain | 149-299 | Aspartate/ornithine carbamoyltransferase Asp/Orn-binding | |||
Sequence similarities
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length306
- Mass (Da)34,165
- Last updated2023-05-03 v1
- MD5 ChecksumCD98E22FCBA6FDB7EEDA10B732CC1B25
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DVGK01000027 EMBL· GenBank· DDBJ | HIR12626.1 EMBL· GenBank· DDBJ | Genomic DNA |