Q9ZPF5 · ARGI2_ARATH
- ProteinArginase 2, chloroplastic/mitochondrial
- GeneARGAH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids344 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolysis of L-arginine to urea and L-ornithine. The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline (By similarity).
Possesses agmatinase activity. Catalyzes the formation of putrescine from agmatine (PubMed:28716421).
Possesses agmatinase activity. Catalyzes the formation of putrescine from agmatine (PubMed:28716421).
Miscellaneous
Plants over-expressing ARGAH2 have decreased susceptibility to the fungal pathogen B.cinerea.
Catalytic activity
- H2O + L-arginine = L-ornithine + urea
Cofactor
Note: Binds 2 manganese ions per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
72.6 μM | agmatine |
Pathway
Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 163 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 187 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 187 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 189 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 189-193 | substrate | ||||
Sequence: HPDIY | ||||||
Binding site | 191 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 197-199 | substrate | ||||
Sequence: EGN | ||||||
Binding site | 228 | substrate | ||||
Sequence: N | ||||||
Binding site | 272 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 272 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 274 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 315 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | agmatinase activity | |
Molecular Function | arginase activity | |
Molecular Function | cobalt ion binding | |
Biological Process | defense response to fungus | |
Biological Process | ornithine metabolic process | |
Biological Process | proline metabolic process | |
Biological Process | putrescine biosynthetic process | |
Biological Process | putrescine biosynthetic process from arginine, using agmatinase | |
Biological Process | putrescine metabolic process | |
Biological Process | tyrosine metabolic process | |
Biological Process | urea cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArginase 2, chloroplastic/mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9ZPF5
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Increased formation of lateral and adventitious roots and increased production of NO in roots.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 40 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-26 | Chloroplast and mitochondrion | ||||
Sequence: MWKIGQRGVPYFQRLIAAPFTTLRSL | ||||||
Chain | PRO_0000173704 | 27-344 | Arginase 2, chloroplastic/mitochondrial | |||
Sequence: PTSLVETGQNRVIDASLTLIRERAKLKGELVRLIGGAKATTALLGVPLGHNSSFLEGPALAPPHVREAIWCGSTNSTTEEGKELKDPRVLSDVGDIPVQEIREMGVDDDRLMKVVSESVKLVMEEEPLRPLVIGGDHSISYPVVRAVSEKLGGPVDILHLDAHPDIYDRFEGNYYSHASSFARIMEGGYARRLLQVGIRSINKEGREQGKRFGVEQYEMRTFSKDRQMLENLKLGEGVKGVYISIDVDCLDPGFAHGVSHFEPGGLSFRDVLNILHNLQGDLVGADVVEYNPQRDTADDMTAMVAAKFVRELAAKMSK |
Proteomic databases
Expression
Tissue specificity
Expressed in vasculature of roots, root tips, leaves and cotyledons.
Induction
By methyl jasmonate and infection with the fungal pathogen B.cinerea.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q9ZPF5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length344
- Mass (Da)37,980
- Last updated1999-05-01 v1
- ChecksumFED95D31B1A2FEBE
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B9DFC0 | B9DFC0_ARATH | ARGAH2 | 263 |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF128396 EMBL· GenBank· DDBJ | AAD17371.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161513 EMBL· GenBank· DDBJ | CAB78011.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE82684.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT003815 EMBL· GenBank· DDBJ | AAO41868.1 EMBL· GenBank· DDBJ | mRNA |