A0A5C6LVX6 · A0A5C6LVX6_9BACT
- ProteinAspartate carbamoyltransferase
- GenepyrB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids313 (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 | 58 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 59 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 86 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 108 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 136 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 139 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 169 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 224 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 265 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 266 | 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 > Bacteroidota > Chitinophagia > Chitinophagales > Chitinophagaceae > Chitinophaga
Accessions
- Primary accessionA0A5C6LVX6
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).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-149 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | |||
Domain | 156-303 | 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
- Length313
- Mass (Da)34,454
- Last updated2019-11-13 v1
- ChecksumF77F59EE83ACCC14
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VOHS01000015 EMBL· GenBank· DDBJ | TWV99525.1 EMBL· GenBank· DDBJ | Genomic DNA |