P00812 · ARGI_YEAST
- ProteinArginase
- GeneCAR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids333 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Miscellaneous
Present with 42800 molecules/cell in log phase SD medium.
Catalytic activity
- H2O + L-arginine = L-ornithine + urea
Cofactor
Note: Binds 2 manganese ions per subunit.
Pathway
Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 123 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 146 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 146 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 148 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 148-152 | substrate | ||||
Sequence: HADIN | ||||||
Binding site | 150 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 159-161 | substrate | ||||
Sequence: SGN | ||||||
Binding site | 205 | substrate | ||||
Sequence: D | ||||||
Binding site | 256 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 256 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 258 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 270 | substrate | ||||
Sequence: T | ||||||
Binding site | 301 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mating projection tip | |
Cellular Component | nucleus | |
Cellular Component | ornithine carbamoyltransferase inhibitor complex | |
Molecular Function | arginase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | ornithine carbamoyltransferase inhibitor activity | |
Molecular Function | zinc ion binding | |
Biological Process | arginine catabolic process to ornithine | |
Biological Process | regulation of ornithine metabolic process | |
Biological Process | urea cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameArginase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP00812
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000173711 | 1-333 | Arginase | |||
Sequence: METGPHYNYYKNRELSIVLAPFSGGQGKLGVEKGPKYMLKHGLQTSIEDLGWSTELEPSMDEAQFVGKLKMEKDSTTGGSSVMIDGVKAKRADLVGEATKLVYNSVSKVVQANRFPLTLGGDHSIAIGTVSAVLDKYPDAGLLWIDAHADINTIESTPSGNLHGCPVSFLMGLNKDVPHCPESLKWVPGNLSPKKIAYIGLRDVDAGEKKILKDLGIAAFSMYHVDKYGINAVIEMAMKAVHPETNGEGPIMCSYDVDGVDPLYIPATGTPVRGGLTLREGLFLVERLAESGNLIALDVVECNPDLAIHDIHVSNTISAGCAIARCALGETLL | ||||||
Modified residue | 16 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 77 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 270 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By arginine or homoarginine.
Interaction
Subunit
Homotrimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P00812 | ARG3 P05150 | 4 | EBI-2856, EBI-12712 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length333
- Mass (Da)35,662
- Last updated1986-07-21 v1
- ChecksumA5979DC9F1FDFF2E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M10414 EMBL· GenBank· DDBJ | AAA34470.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43503 EMBL· GenBank· DDBJ | AAB68250.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M10110 EMBL· GenBank· DDBJ | AAA34469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11322.1 EMBL· GenBank· DDBJ | Genomic DNA |