Q8I384 · ARGI_PLAF7
- ProteinArginase
- GeneARG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids411 (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:15843155, PubMed:19456858, PubMed:20527960, PubMed:21728378).
May play a role in parasite intra-hepatic development during the host liver stage (By similarity).
May play a role in parasite intra-hepatic development during the host liver stage (By similarity).
Catalytic activity
- H2O + L-arginine = L-ornithine + urea
Cofactor
Note: Binds 2 manganese ions per subunit.
Activity regulation
Feedback inhibition by product L-ornithine, (PubMed:15843155).
Inhibited by 2(S)-amino-6-boronohexanoic acid (ABH); however, with less efficiency than human ARG1 (PubMed:20527960, PubMed:21728378).
Inhibited by 2(S)-amino-6-boronohexanoic acid (ABH); however, with less efficiency than human ARG1 (PubMed:20527960, PubMed:21728378).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3 mM | L-arginine | 8 | 37 | |||
3.3 mM | L-arginine | 8.5 | 37 | |||
4 mM | L-arginine | 8 | 37 | |||
25 mM | L-arginine | 7.4 | 37 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
31 μmol/min/mg | 8 | 37 |
kcat is 440 sec-1 with L-arginine as substrate (at pH 8.5 and 37 degrees Celsius) (PubMed:20527960).
kcat is 96 sec-1 with L-arginine as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15843155).
kcat is 320 sec-1 with L-arginine as substrate (at pH 8 and 37 degrees Celsius) (PubMed:20527960).
kcat is 77 sec-1 with L-arginine as substrate (at pH 7.4 and 37 degrees Celsius) (PubMed:20527960).
kcat is 96 sec-1 with L-arginine as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15843155).
kcat is 320 sec-1 with L-arginine as substrate (at pH 8 and 37 degrees Celsius) (PubMed:20527960).
kcat is 77 sec-1 with L-arginine as substrate (at pH 7.4 and 37 degrees Celsius) (PubMed:20527960).
pH Dependence
Optimum pH is 8.5-9.
Temperature Dependence
Stable up to 57 degrees Celsius.
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 | 193 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 216 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 216 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 218 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 220 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 222 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 229 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 274 | L-arginine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 325 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
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 namesPFA ; PfArg
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8I384
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 193 | Loss of catalytic activity. No defect in oligomerization. | ||||
Sequence: H → A | ||||||
Mutagenesis | 216 | Loss of catalytic activity. Loss of oligomerization. | ||||
Sequence: D → A | ||||||
Mutagenesis | 218 | Loss of catalytic activity. Loss of oligomerization. | ||||
Sequence: H → A | ||||||
Mutagenesis | 220 | Loss of catalytic activity. Loss of oligomerization. | ||||
Sequence: D → A | ||||||
Mutagenesis | 233 | Loss of catalytic activity. Loss of oligomerization. | ||||
Sequence: H → A | ||||||
Mutagenesis | 295 | Severe loss of catalytic activity. Oligomerization is partially reduced. | ||||
Sequence: E → A | ||||||
Mutagenesis | 295 | 11-fold reduction in affinity for L-arginine. Loss of oligomerization. | ||||
Sequence: E → R | ||||||
Mutagenesis | 323 | Loss of catalytic activity and loss of oligomerization; when associated with A-325. | ||||
Sequence: D → A | ||||||
Mutagenesis | 325 | Loss of catalytic activity and loss of oligomerization; when associated with A-323. | ||||
Sequence: D → A | ||||||
Mutagenesis | 347 | Severe loss of catalytic activity. Loss of oligomerization. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 381 | 2.5-fold decrease in affinity for L-arginine. | ||||
Sequence: H → A | ||||||
Mutagenesis | 404 | 3.4-fold reduction in affinity for L-arginine. Loss of oligomerization. | ||||
Sequence: R → A |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000457081 | 1-411 | UniProt | Arginase | |||
Sequence: MLDTIESYIKSHKEKENLYVKKNVSIIGSPLAAGQPLGGVQLACDDLRKLGLHNVIDVLGWKYEDIGNIDNGDNEMKQEKKTNNYINNNDNNNDNNNDNNNDNNNNCYIPNGVIKEKKHDLSNNKMNGYVNHNFYGNYEENNVISTNDKYKNNCYYDNIRNIKEIGIFSKNLFDTMSNELRKKNFVLNIGGDHGVAFSSILSSLQMYQNLRVIWIDAHGDINIPETSPSGNYHGMTLAHTLGLFKKKVPYFEWSENLTYLKPENTAIIGIRDIDAYEKIILKKCNINYYTIFDIEKNGIYNTICTALEKIDPNSNCPIHISLDIDSVDNVFAPGTGTVAKGGLNYREINLLMKILAETKRVVSMDLVEYNPSLDEVDKKVHGDSLPILDNATKTGKLCLELIARVLGYDIV | |||||||
Modified residue (large scale data) | 122 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 372 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Developmental stage
Expressed during the asexual blood stage; expression is high in rings and young trophozoites, and low in mature trophozoites and schizonts.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 83-106 | Disordered | ||||
Sequence: NNYINNNDNNNDNNNDNNNDNNNN |
Sequence similarities
Belongs to the arginase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length411
- Mass (Da)46,493
- Last updated2003-03-01 v1
- Checksum38886C355CC745F7
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 256 | in Ref. 1; CAC86388 | ||||
Sequence: N → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ313518 EMBL· GenBank· DDBJ | CAC86388.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL844508 EMBL· GenBank· DDBJ | CAD51750.1 EMBL· GenBank· DDBJ | Genomic DNA |