C9RKD9 · C9RKD9_FIBSS
- ProteinAspartate carbamoyltransferase
- GenepyrB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids313 (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 | 59 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 60 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 87 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 109 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 137 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 140 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 170 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 225 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 266 | carbamoyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 267 | 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
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Fibrobacterota > Fibrobacteria > Fibrobacterales > Fibrobacteraceae > Fibrobacter
Accessions
- Primary accessionC9RKD9
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).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-150 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | |||
Domain | 156-303 | Aspartate/ornithine carbamoyltransferase Asp/Orn-binding | |||
Sequence similarities
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length313
- Mass (Da)34,525
- Last updated2009-11-24 v1
- MD5 ChecksumCA7DB91119E5212D838D1919D208704B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002158 EMBL· GenBank· DDBJ | ADL25889.1 EMBL· GenBank· DDBJ | Genomic DNA |