A0A6G4Z527 · A0A6G4Z527_STAAU
- ProteinAspartate carbamoyltransferase
- GenepyrB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids293 (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 | 50 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 78 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 100 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 127 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 130 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 160 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 210 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 253 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 254 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: P |
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 > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A6G4Z527
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 | 3-140 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | ||||
Sequence: HLLSMEHLSTDQIYKLIQKASQFKSGERQLPNFEGEYVANLFFENSTRTKCSFEMAELKLGLKTISFETSTSSVSKGESLYDTCKTLESIGCDLLVIRHPFNNYYEKLANINIPIANAGDGSGQHPTQSLLDLMTIYE | ||||||
Domain | 146-288 | Aspartate/ornithine carbamoyltransferase Asp/Orn-binding | ||||
Sequence: EGLNVLICGDIKNSRVARSNYHSLKALGANVMFNSPNAWIDDSLEAPYVNIDDVIETVDIVMLLRIQHERHGLAEETRFAADDYHQKHGLNEVRYNKLQEHAIVMHPAPVNRGVEIQSDLVEASKSRIFKQMENGVYLRMAVI |
Sequence similarities
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length293
- Mass (Da)33,259
- Last updated2020-08-12 v1
- Checksum345C67C203DAFE24