B7LMR8 · PYRB_ESCF3
- ProteinAspartate carbamoyltransferase catalytic subunit
- GenepyrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids311 (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 | 85 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 106 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 135 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 138 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 168 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 230 | 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 catalytic subunit
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionB7LMR8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_1000191909 | 1-311 | Aspartate carbamoyltransferase catalytic subunit | ||
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
Sequence
- Sequence statusComplete
- Length311
- Mass (Da)34,485
- Last updated2009-02-10 v1
- ChecksumC387FA6B6B10C8E0
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU928158 EMBL· GenBank· DDBJ | CAQ91746.1 EMBL· GenBank· DDBJ | Genomic DNA |