C4LSS0 · ARGI_ENTH1
- ProteinArginase
- GeneARG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids296 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis (PubMed:15053781, PubMed:29691540, PubMed:31199070).
By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune response (PubMed:15053781).
By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune response (PubMed:15053781).
Catalytic activity
- H2O + L-arginine = L-ornithine + urea
Cofactor
Note: Binds 2 manganese ions per subunit.
Activity regulation
Substitution of the loosely bound surface exposed Mn2+ with Mg2+, Zn2+, Ni2+ or Co2+ results in similar catalytic activity, substitution with Cd2+ and Cu2+ reduces catalytic activity and substitution with Hg2+ and Ca2+ inhibits the enzyme (PubMed:29691540).
Inhibited by L-norvaline (PubMed:15053781, PubMed:29691540).
Inhibited by L-norvaline (PubMed:15053781, PubMed:29691540).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
137 mM | L-arginine | 7.5 | 37 |
pH Dependence
Optimum pH is 8.5-9.
Temperature Dependence
Optimum temperature is 55 degrees Celsius (PubMed:29691540).
Active up to 70 degrees Celsius (PubMed:29691540).
Active up to 70 degrees Celsius (PubMed:29691540).
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 | 98 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 124 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 124 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 126 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 130 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 137 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 178 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 225 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 225 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 227 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 227 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 239 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | arginase activity | |
Molecular Function | identical protein binding | |
Molecular Function | manganese ion binding | |
Biological Process | arginine catabolic process to ornithine | |
Biological Process | urea cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArginase
- EC number
- Short namesEhArg
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Archamoebae > Mastigamoebida > Entamoebidae > Entamoeba
Accessions
- Primary accessionC4LSS0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000457083 | 1-296 | Arginase | |||
Sequence: MQFEKVTYIAVPQKYGQKKVGVEEGPKFLEKLGFMNVLEQVAKSVNKKTITEPKTPQELGVTNARNLNEVESVNIELRDTIAKEYDVNNLLINIGGDHSIGLGTIAGVVKAMKPNARVGVVWFDAHPDMNTPENSPSGNIHGMPLACAVGLGPQRLTSIMPHYITPKDIMYVGIRSIDVGEQFEIQDKHIDHFTAEDVKRVGMKEVIEAINKKFVDYDVIHLSFDIDGIDPEFILGTGTPVPKGISLEDSLYFMSEMGKMKKLHSVDIVEYNPKIEEEITGKNVLKCISSLFGIKC |
Structure
Sequence
- Sequence statusComplete
- Length296
- Mass (Da)32,844
- Last updated2009-07-07 v1
- ChecksumE5AE498FB991DE4D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS571145 EMBL· GenBank· DDBJ | EAL51512.1 EMBL· GenBank· DDBJ | Genomic DNA |