Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Analysis of Arabidopsis arginase gene transcription patterns indicates specific biological functions for recently diverged paralogs.
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ARGAH hydrolyzes arginine to ornithine and urea.
"We
demonstrated tissue-specific transcript expression and enzyme activity in pollen
for ARGAH1, but not ARGAH2."
Divalent metal ions in plant mitochondria and their role in interactions with proteins and oxidative stress-induced damage to respiratory function.
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The metal-affinity screen suggests association, but target-specific direct binding remains unresolved.
"The interaction of metal ions with mitochondrial proteins that might be responsible for these toxic effects was investigated in vitro using IMAC to trap metal-binding proteins."
Dual functioning of plant arginases provides a third route for putrescine synthesis.
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ARGAH also catalyzes agmatine hydrolysis to putrescine.
"Transformation of Arabidopsis thaliana ADC2, and any of the arginases from A.
thaliana (ARGAH1, or ARGHA2) or the soybean gene Glyma.03g028000 (GmARGAH) into
a yeast strain deficient in ODC, fully complemented the mutant phenotype."
Global Analysis of Membrane-associated Protein Oligomerization Using Protein Correlation Profiling.
The Neighboring Subunit Is Engaged to Stabilize the Substrate in the Active Site of Plant Arginases.
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The reported structural cofactor is manganese, not magnesium.
"The active site with a double manganese cluster is formed in each ARGAH subunit"
Nucleotide sequence of Arabidopsis thaliana arginase expressed in yeast.
Ornithine-delta-aminotransferase is essential for arginine catabolism but not for proline biosynthesis.
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Arginase supplies the arginine-cleavage arm of ornithine/arginine recycling.
"Accumulation of Cit indicated that Orn and Arg were metabolised after uptake, most likely by enzymes of the urea cycle."
UniProt record for ARGAH1
Source-specific Arabidopsis localization audit
Arginase-negative mutants of Arabidopsis exhibit increased nitric oxide signaling in root development.
Reproducible Figure 2 localization evidence for Arabidopsis ARGAH1 and ARGAH2
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Both tagged Arabidopsis arginases localize to the mitochondrial interior in tobacco BY-2 cells, supported by marker colocalization and selective permeabilization.
"Therefore, each protein was actually localized in the mitochondrial interior (matrix)"