C0QVX1 · PYRB_BRAHW
- ProteinAspartate carbamoyltransferase catalytic subunit
- GenepyrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids359 (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 = H+ + N-carbamoyl-L-aspartate + phosphate
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 | 52 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 53 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 81 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 102 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 130 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 133 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 163 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 224 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 264 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 265 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: P |
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 catalytic subunit
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Spirochaetota > Spirochaetia > Brachyspirales > Brachyspiraceae > Brachyspira
Accessions
- Primary accessionC0QVX1
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000201585 | 1-359 | Aspartate carbamoyltransferase catalytic subunit | |||
Sequence: MRNFISIKELSKEEVIEVLDVAKELDNADSKERRKIMDGMIMTSIFFEPSTRTRLSFTSAAYRLGCKELGFDNPEQSSVKKGESLRDTIIMVSAYSDIIVMRHSIDGAAKFAEEVTNCPIINAGDGANEHPSQTLLDLYTLREELGTIENQKVAFVGDTRYGRTVHSLVDGLMMFNGQFYFISPDVIQIPDYILKELDNANIKYKKLSNYEEVLKEIDCLYMTRVQRERFDDINEYEEVKHAFRISKDNIVGKCKDDMIILHPLPRVDEINIDLDDTKYAKYFIQARNGVPTRMAMMALATDAIKSKVKRKEMNYEVVENKEVVCPNNKCVTHFEETKNRVVKKGYGDFCYYCNREIGK |
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
Sequence
- Sequence statusComplete
- Length359
- Mass (Da)41,346
- Last updated2009-05-05 v1
- ChecksumC7FEA811FA894089
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001357 EMBL· GenBank· DDBJ | ACN82549.1 EMBL· GenBank· DDBJ | Genomic DNA |