A0A0Q7AST6 · A0A0Q7AST6_9ACTN
- ProteinAspartate carbamoyltransferase
- GenepyrB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids318 (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 | 55 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 56 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 83 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 105 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 135 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 138 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 173 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 227 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 268 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 269 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Nocardioides
Accessions
- Primary accessionA0A0Q7AST6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-147 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | |||
Domain | 160-306 | Aspartate/ornithine carbamoyltransferase Asp/Orn-binding | |||
Sequence similarities
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length318
- Mass (Da)34,256
- Last updated2016-01-20 v1
- Checksum4616E89E149A6E4B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LMDV01000014 EMBL· GenBank· DDBJ | KQW43074.1 EMBL· GenBank· DDBJ | Genomic DNA |