A0A225CA80 · A0A225CA80_9MICO
- ProteinAspartate carbamoyltransferase
- GenepyrB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids318 (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 | 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 | 134 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 137 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 174 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 230 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 271 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 272 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Clavibacter
Accessions
- Primary accessionA0A225CA80
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 | 2-146 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | ||||
Sequence: RHLLSTRDLSRDEAVHILDVAEDMADVGTREIKKTPALRGRTVVNLFFEDSTRTRISFEAAAKRLSADVINFSAKGSSVSKGESLKDTAQTLQAMGADGVVVRHPSSGAPHTLAGSGWIDAGIVNAGDGTHEHPTQALLDAFTIR | ||||||
Domain | 161-309 | Aspartate/ornithine carbamoyltransferase Asp/Orn-binding | ||||
Sequence: GTRVVIVGDVLHSRVARSNAWLLTTLGAEVTLVAPPTLVPVGVGSWPVQVRYDLDAALVEGKPDAVMMLRIQAERMRAAFFPNPREYARIWGLDDARLALLGPDTIVMHPGPMNRGLEISAAAADSERSTVREQVANGVSVRMAVLYLL |
Sequence similarities
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length318
- Mass (Da)34,092
- Last updated2017-10-25 v1
- Checksum75A2BFADDBAD26E8