A0A3D8R8V7 · A0A3D8R8V7_9EURO
- ProteinProtein pyrABCN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2268 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 357 | Nucleophile | |||
Active site | 441 | ||||
Active site | 443 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | dihydroorotase activity | |
Molecular Function | metal ion binding | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | citrulline biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | UTP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA0A3D8R8V7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 619-811 | ATP-grasp | |||
Domain | 1154-1345 | ATP-grasp | |||
Domain | 1411-1590 | MGS-like | |||
Region | 1881-1910 | Disordered | |||
Sequence similarities
In the 2nd section; belongs to the CarB family.
In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
In the N-terminal section; belongs to the CarA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,268
- Mass (Da)248,819
- Last updated2019-01-16 v1
- Checksum3A63A5F895033756
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PVWQ01000010 EMBL· GenBank· DDBJ | RDW70489.1 EMBL· GenBank· DDBJ | Genomic DNA |