ASP2 encodes the major cytosolic aspartate aminotransferase activity AAT2 in Arabidopsis. This pyridoxal-phosphate enzyme reversibly transfers nitrogen between glutamate and aspartate, coupling oxaloacetate and 2-oxoglutarate metabolism to nitrogen assimilation and the supply of aspartate for asparagine formation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000325 plant-type vacuole | HDA PMID:17151019 A proteomics dissection of Arabidopsis thaliana vacuoles iso... | UNDECIDED | Summary: Plant-type vacuole assignment needs target-specific resolution. Reason: PMID:17151019 is a compartment proteomics/localization source. The exact ASP2 evidence establishing plant-type vacuole residence rather than co-purification was not independently recovered. Established localization elsewhere does not exclude a minor or conditional pool; no absence is asserted. Supporting Evidence: |
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: Use the directly demonstrated aminotransferase activities. Reason: General catalysis/transamination is correct but less informative than the supported specific reactions. Proposed replacements: L-aspartate:2-oxoglutarate transaminase activity Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | IBA GO_REF:0000033 | ACCEPT | Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination. Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates file:ARATH/ASP2/ASP2-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | IDA PMID:9535706 Recombinant expression, purification, and characterization o... | ACCEPT | Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination. Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates file:ARATH/ASP2/ASP2-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination. Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates file:ARATH/ASP2/ASP2-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | ISS GO_REF:0000024 | ACCEPT | Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination. Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates file:ARATH/ASP2/ASP2-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0005507 copper ion binding | HDA PMID:20018591 Divalent metal ions in plant mitochondria and their role in ... | UNDECIDED | Summary: Copper ion binding assignment needs target-specific resolution. Reason: PMID:20018591 reports immobilized-metal affinity capture. The exact ASP2 copper-capture data could not be independently resolved; PLP dependence does not rule out auxiliary copper binding. Supporting Evidence: |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | MODIFY | Summary: ASP2 is the major cytosolic AAT2 isozyme. Reason: Recombinant/native isozyme comparison in PMID:9535706 and native mutant analysis in PMID:12068109 independently establish cytosolic function. Refine broad cytoplasm to the already supported cytosol. Proposed replacements: cytosol Supporting Evidence: PMID:12068109 sequencing of the ASP2 gene from the cytosolic aat2 mutants |
| GO:0005737 cytoplasm | ISM GO_REF:0000122 | MODIFY | Summary: ASP2 is the major cytosolic AAT2 isozyme. Reason: Recombinant/native isozyme comparison in PMID:9535706 and native mutant analysis in PMID:12068109 independently establish cytosolic function. Refine broad cytoplasm to the already supported cytosol. Proposed replacements: cytosol Supporting Evidence: PMID:12068109 sequencing of the ASP2 gene from the cytosolic aat2 mutants |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | UNDECIDED | Summary: Mitochondrion assignment needs target-specific resolution. Reason: The PAINT mitochondrial assignment remains unresolved against direct cytosolic isozyme evidence; no target-specific mitochondrial activity or import assay was recovered. Cytosolic localization alone does not prove mitochondrial exclusion. Propagation Review Root cause: UNRESOLVED Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN000222845 UNRESOLVED The proximate PAINT node is preserved. Target ASP2 is experimentally cytosolic; whether the ancestral mitochondrial assignment also holds for a minor target pool remains unresolved. No source annotation is declared false. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0005794 Golgi apparatus | RCA NOT PMID:22430844 Isolation and proteomic characterization of the Arabidopsis ... | UNDECIDED | Summary: The ASP2 localization exclusion remains unresolved. Reason: The seeded annotation explicitly excludes Golgi localization. Native cytosolic ASP2 activity is established, but the exact target-specific fractionation and exclusion evidence in PMID:22430844 could not be resolved from the inspected material; supplementary download attempts failed. Cytosolic residence alone does not prove absence from Golgi. Supporting Evidence: |
| GO:0005829 cytosol | HDA PMID:25293756 A proteomic strategy for global analysis of plant protein co... | ACCEPT | Summary: ASP2 is the major cytosolic AAT2 isozyme. Reason: Recombinant/native isozyme comparison in PMID:9535706 and native mutant analysis in PMID:12068109 independently establish cytosolic function. Refine broad cytoplasm to the already supported cytosol. Supporting Evidence: PMID:12068109 sequencing of the ASP2 gene from the cytosolic aat2 mutants |
| GO:0005829 cytosol | IDA PMID:7894512 The aspartate aminotransferase gene family of Arabidopsis en... | ACCEPT | Summary: ASP2 is the major cytosolic AAT2 isozyme. Reason: Recombinant/native isozyme comparison in PMID:9535706 and native mutant analysis in PMID:12068109 independently establish cytosolic function. Refine broad cytoplasm to the already supported cytosol. Supporting Evidence: PMID:12068109 sequencing of the ASP2 gene from the cytosolic aat2 mutants |
| GO:0005886 plasma membrane | HDA PMID:17644812 A high content in lipid-modified peripheral proteins and int... | UNDECIDED | Summary: Plasma membrane assignment needs target-specific resolution. Reason: PMID:17644812 is a compartment proteomics/localization source. The exact ASP2 evidence establishing plasma membrane residence rather than co-purification was not independently recovered. Established localization elsewhere does not exclude a minor or conditional pool; no absence is asserted. Supporting Evidence: |
| GO:0006103 2-oxoglutarate metabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: The transaminase directly metabolizes this reaction substrate/product. Reason: The measured reversible reaction interconverts aspartate, glutamate, oxaloacetate and 2-oxoglutarate. Native evidence in PMID:12068109 supports physiological Asp-family metabolism without requiring every mutant to be a complete null. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0006520 amino acid metabolic process | IEA GO_REF:0000002 | MODIFY | Summary: Specify the experimentally grounded amino-acid processes. Reason: For ASP2/ASP5 the reversible AspAT reaction directly metabolizes Asp and Glu. PAT additionally catalyzes arogenate formation in phenylalanine biosynthesis; broad precursor supply alone does not establish every downstream pathway. Proposed replacements: aspartate metabolic process glutamate metabolic process Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0006531 aspartate metabolic process | IMP PMID:9611168 Arabidopsis mutants define an in vivo role for isoenzymes of... | ACCEPT | Summary: The transaminase directly metabolizes this reaction substrate/product. Reason: The measured reversible reaction interconverts aspartate, glutamate, oxaloacetate and 2-oxoglutarate. Native evidence in PMID:12068109 supports physiological Asp-family metabolism without requiring every mutant to be a complete null. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0006531 aspartate metabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: The transaminase directly metabolizes this reaction substrate/product. Reason: The measured reversible reaction interconverts aspartate, glutamate, oxaloacetate and 2-oxoglutarate. Native evidence in PMID:12068109 supports physiological Asp-family metabolism without requiring every mutant to be a complete null. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0006536 glutamate metabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: The transaminase directly metabolizes this reaction substrate/product. Reason: The measured reversible reaction interconverts aspartate, glutamate, oxaloacetate and 2-oxoglutarate. Native evidence in PMID:12068109 supports physiological Asp-family metabolism without requiring every mutant to be a complete null. Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0008483 transaminase activity | IEA GO_REF:0000002 | MODIFY | Summary: Use the directly demonstrated aminotransferase activities. Reason: General catalysis/transamination is correct but less informative than the supported specific reactions. Proposed replacements: L-aspartate:2-oxoglutarate transaminase activity Supporting Evidence: PMID:9535706 Kinetic parameters (Km and kcat) obtained for all four substrates |
| GO:0009505 plant-type cell wall | HDA PMID:16287169 Arabidopsis cell wall proteome defined using multidimensiona... | UNDECIDED | Summary: Plant-type cell wall assignment needs target-specific resolution. Reason: PMID:16287169 is a compartment proteomics/localization source. The exact ASP2 evidence establishing plant-type cell wall residence rather than co-purification was not independently recovered. Established localization elsewhere does not exclude a minor or conditional pool; no absence is asserted. Supporting Evidence: |
| GO:0009506 plasmodesma | HDA PMID:21533090 Arabidopsis plasmodesmal proteome. | UNDECIDED | Summary: Plasmodesma assignment needs target-specific resolution. Reason: PMID:21533090 Supplement S3 directly detects ASP2 peptides, while S4 classifies it NSnoTM. The study acknowledges substantial putative cytoplasmic contamination. Detection does not resolve stable plasmodesmal association, and absence of a membrane helix is not exclusion. Supporting Evidence: |
| GO:0009536 plastid | HDA PMID:28887381 Global Analysis of Membrane-associated Protein Oligomerizati... | UNDECIDED | Summary: Plastid assignment needs target-specific resolution. Reason: PMID:28887381 Supplement S1 identifies the ASP2/ASP4 protein group and labels it cytosol; mixed-fraction detection does not independently resolve plastid import. Supporting Evidence: |
| GO:0030170 pyridoxal phosphate binding | IEA GO_REF:0000002 | ACCEPT | Summary: Pyridoxal phosphate is the integral catalytic cofactor. Reason: The conserved PLP-dependent aminotransferase mechanism and curated cofactor information support this core binding property. Supporting Evidence: file:ARATH/ASP2/ASP2-uniprot.txt Name=pyridoxal 5'-phosphate; |
| GO:0071456 cellular response to hypoxia | HEP PMID:31519798 Integrative Analysis from the Epigenome to Translatome Uncov... | KEEP AS NON CORE | Summary: ASP2 expression participates in the measured hypoxia-response program. Reason: PMID:31519798 profiles hypoxia and reoxygenation regulation. Retain the curator-linked expression response as contextual; it does not establish a separate essential hypoxia-tolerance mechanism. Supporting Evidence: PMID:31519798 in response to hypoxia and reoxygenation |
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Download this section (compressed HTML)Q: Which minor compartment assignments represent a stable active enzyme pool rather than transient association or proteomic co-purification?
Experiment: Combine endogenous tagging and controlled fractionation with labeled-substrate/product measurements in wild type, loss-of-function and complemented lines to resolve active compartment pools and physiological reaction direction.
Type: native localization and isotope flux
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