A0AA91TXV8 · A0AA91TXV8_WOLPI
- ProteinAspartate carbamoyltransferase
- GenepyrB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids295 (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.
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
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 | 54 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 55 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 82 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 104 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 132 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 135 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 165 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 218 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 257 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 258 | 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 | amino acid metabolic process | |
Biological Process | pyrimidine ribonucleotide biosynthetic 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 > Pseudomonadota > Alphaproteobacteria > Rickettsiales > Anaplasmataceae > Wolbachieae > Wolbachia
Accessions
- Primary accessionA0AA91TXV8
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 | 5-143 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | ||||
Sequence: RNLLNISDLTIGDVENITKLANQYLEEKVENSHVLKNKIVINLFFEDSTRTLASFEIAAKSLGANVITLPIKSSSINKGEDLKDMIKTLNAMNPDYMIIRHKSSGIINTLAKHVNCSLINAGDGSSEHPTQALADYLVI | ||||||
Domain | 151-291 | Aspartate/ornithine carbamoyltransferase Asp/Orn-binding | ||||
Sequence: KNLKIVICGDILHSRVARSNIRLLKMFGAKISLVAPPALMCKHFSEVDSLHYSLTEGIKDADVIMLLRLQKERMNNNSSEKEYFHLYGLDAQKLSHAKPDAIVMHPGPINRGIEISNDIEDCVILQQVKFGLATRKAVLHY |
Sequence similarities
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length295
- Mass (Da)32,975
- Last updated2024-03-27 v1
- Checksum8F9184336C227B8B