ALAAT1 is a mitochondrial pyridoxal-phosphate-dependent alanine aminotransferase. It reversibly interconverts alanine and 2-oxoglutarate with pyruvate and glutamate and is especially important for alanine utilization during recovery from low oxygen. It also contributes to mitochondrial glyoxylate transamination in a conditional photorespiratory side pathway.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001666 response to hypoxia | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ALAAT1 responds to low oxygen and supports subsequent recovery. Reason: PMID:17319845 documents induction and delayed alanine turnover in the mutant during reoxygenation. PMID:31519798 independently profiles the stress-response program; neither implies that ALAAT1 is universally responsible for hypoxic alanine synthesis. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Rapidly induced upon low-oxygen stress in roots and shoots. |
| GO:0001666 response to hypoxia | IEP PMID:17319845 Alanine aminotransferase catalyses the breakdown of alanine ... | KEEP AS NON CORE | Summary: ALAAT1 responds to low oxygen and supports subsequent recovery. Reason: PMID:17319845 documents induction and delayed alanine turnover in the mutant during reoxygenation. PMID:31519798 independently profiles the stress-response program; neither implies that ALAAT1 is universally responsible for hypoxic alanine synthesis. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Rapidly induced upon low-oxygen stress in roots and shoots. |
| GO:0004021 L-alanine:2-oxoglutarate transaminase activity | IBA GO_REF:0000033 | ACCEPT | Summary: ALAAT1 catalyzes alanine/2-oxoglutarate transamination. Reason: PMID:17319845 native loss-of-function and enzyme assays support the reaction; PMID:22268146 corroborates loss of alanine/2-oxoglutarate activity in ALAAT1-suppressed plants. Purified ALAAT2 profiling is not assigned to ALAAT1. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Reaction=L-alanine + 2-oxoglutarate = pyruvate + L-glutamate; |
| GO:0004021 L-alanine:2-oxoglutarate transaminase activity | IDA PMID:17319845 Alanine aminotransferase catalyses the breakdown of alanine ... | ACCEPT | Summary: ALAAT1 catalyzes alanine/2-oxoglutarate transamination. Reason: PMID:17319845 native loss-of-function and enzyme assays support the reaction; PMID:22268146 corroborates loss of alanine/2-oxoglutarate activity in ALAAT1-suppressed plants. Purified ALAAT2 profiling is not assigned to ALAAT1. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Reaction=L-alanine + 2-oxoglutarate = pyruvate + L-glutamate; |
| GO:0004021 L-alanine:2-oxoglutarate transaminase activity | IEA GO_REF:0000120 | ACCEPT | Summary: ALAAT1 catalyzes alanine/2-oxoglutarate transamination. Reason: PMID:17319845 native loss-of-function and enzyme assays support the reaction; PMID:22268146 corroborates loss of alanine/2-oxoglutarate activity in ALAAT1-suppressed plants. Purified ALAAT2 profiling is not assigned to ALAAT1. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Reaction=L-alanine + 2-oxoglutarate = pyruvate + L-glutamate; |
| GO:0005524 ATP binding | HDA PMID:17137349 Analysis of the soluble ATP-binding proteome of plant mitoch... | UNDECIDED | Summary: ATP binding remains unresolved at the target level. Reason: PMID:17137349 captures soluble mitochondrial proteins on immobilized ATP. Publisher and supplement access failed, preventing independent resolution of ALAAT1 direct binding versus co-capture. PLP-dependent catalysis does not disprove auxiliary ATP interaction. Supporting Evidence: PMID:17137349 captured using immobilized ATP |
| GO:0005634 nucleus | HDA PMID:28887381 Global Analysis of Membrane-associated Protein Oligomerizati... | UNDECIDED | Summary: The nuclear assignment is not independently resolved by the cited proteomics. Reason: PMID:28887381 Supplement S1 lists an ALAAT1/ALAAT2 group as mitochondrial. Mixed protein-correlation fractions do not establish an ALAAT1 nuclear pool; mitochondrial targeting also does not establish its absence. Supporting Evidence: |
| GO:0005739 mitochondrion | HDA PMID:11743115 Analysis of the Arabidopsis mitochondrial proteome. | ACCEPT | Summary: ALAAT1 is targeted to mitochondria. Reason: Multiple mitochondrial proteomes are corroborated by full text of PMID:22268146 ALAAT1-RFP/MitoTracker colocalization. The latter separately tests ALAAT1 and ALAAT2, so the assignment does not rest only on shared peptides. Supporting Evidence: PMID:22268146 Targeting of both enzymes to mitochondria was verified by C-terminal fusion to RFP |
| GO:0005739 mitochondrion | HDA PMID:14671022 Experimental analysis of the Arabidopsis mitochondrial prote... | ACCEPT | Summary: ALAAT1 is targeted to mitochondria. Reason: Multiple mitochondrial proteomes are corroborated by full text of PMID:22268146 ALAAT1-RFP/MitoTracker colocalization. The latter separately tests ALAAT1 and ALAAT2, so the assignment does not rest only on shared peptides. Supporting Evidence: PMID:22268146 Targeting of both enzymes to mitochondria was verified by C-terminal fusion to RFP |
| GO:0005739 mitochondrion | HDA PMID:17137349 Analysis of the soluble ATP-binding proteome of plant mitoch... | ACCEPT | Summary: ALAAT1 is targeted to mitochondria. Reason: Multiple mitochondrial proteomes are corroborated by full text of PMID:22268146 ALAAT1-RFP/MitoTracker colocalization. The latter separately tests ALAAT1 and ALAAT2, so the assignment does not rest only on shared peptides. Supporting Evidence: PMID:22268146 Targeting of both enzymes to mitochondria was verified by C-terminal fusion to RFP |
| GO:0005739 mitochondrion | HDA PMID:18385124 Heterogeneity of the mitochondrial proteome for photosynthet... | ACCEPT | Summary: ALAAT1 is targeted to mitochondria. Reason: Multiple mitochondrial proteomes are corroborated by full text of PMID:22268146 ALAAT1-RFP/MitoTracker colocalization. The latter separately tests ALAAT1 and ALAAT2, so the assignment does not rest only on shared peptides. Supporting Evidence: PMID:22268146 Targeting of both enzymes to mitochondria was verified by C-terminal fusion to RFP |
| GO:0005739 mitochondrion | HDA PMID:25293756 A proteomic strategy for global analysis of plant protein co... | ACCEPT | Summary: ALAAT1 is targeted to mitochondria. Reason: Multiple mitochondrial proteomes are corroborated by full text of PMID:22268146 ALAAT1-RFP/MitoTracker colocalization. The latter separately tests ALAAT1 and ALAAT2, so the assignment does not rest only on shared peptides. Supporting Evidence: PMID:22268146 Targeting of both enzymes to mitochondria was verified by C-terminal fusion to RFP |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: ALAAT1 is targeted to mitochondria. Reason: Multiple mitochondrial proteomes are corroborated by full text of PMID:22268146 ALAAT1-RFP/MitoTracker colocalization. The latter separately tests ALAAT1 and ALAAT2, so the assignment does not rest only on shared peptides. Supporting Evidence: PMID:22268146 Targeting of both enzymes to mitochondria was verified by C-terminal fusion to RFP |
| GO:0005739 mitochondrion | ISM GO_REF:0000122 | ACCEPT | Summary: ALAAT1 is targeted to mitochondria. Reason: Multiple mitochondrial proteomes are corroborated by full text of PMID:22268146 ALAAT1-RFP/MitoTracker colocalization. The latter separately tests ALAAT1 and ALAAT2, so the assignment does not rest only on shared peptides. Supporting Evidence: PMID:22268146 Targeting of both enzymes to mitochondria was verified by C-terminal fusion to RFP |
| GO:0005829 cytosol | RCA NOT PMID:21166475 Analysis of the Arabidopsis cytosolic proteome highlights su... | UNDECIDED | Summary: A physiological cytosolic ALAAT1 pool remains unresolved. Reason: PMID:21166475 is a cytosolic proteome source, while PMID:22268146 directly shows mitochondrial targeting. The exact fractionation/assignment for ALAAT1 and evidence for dual localization could not be resolved; no exclusion from cytosol is asserted. Supporting Evidence: |
| GO:0008483 transaminase activity | IEA GO_REF:0000002 | MODIFY | Summary: Specify alanine/2-oxoglutarate transamination. Reason: The general molecular function can be refined to its directly supported specific reaction. Proposed replacements: L-alanine:2-oxoglutarate transaminase activity Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Reaction=L-alanine + 2-oxoglutarate = pyruvate + L-glutamate; |
| GO:0030170 pyridoxal phosphate binding | IEA GO_REF:0000002 | ACCEPT | Summary: PLP binding is integral to ALAAT1 catalysis. Reason: The conserved class-I aminotransferase cofactor architecture and curated cofactor assignment support this core property, independently of possible auxiliary nucleotide interactions. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Name=pyridoxal 5'-phosphate; |
| GO:0042853 L-alanine catabolic process | IEA GO_REF:0000041 | ACCEPT | Summary: ALAAT1 catalyzes alanine breakdown. Reason: Native evidence in PMID:17319845 loss-of-function delays removal of accumulated alanine after hypoxia; the reaction consumes alanine to produce pyruvate and glutamate. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt the conversion of alanine to pyruvate |
| GO:0042853 L-alanine catabolic process | IMP PMID:17319845 Alanine aminotransferase catalyses the breakdown of alanine ... | ACCEPT | Summary: ALAAT1 catalyzes alanine breakdown. Reason: Native evidence in PMID:17319845 loss-of-function delays removal of accumulated alanine after hypoxia; the reaction consumes alanine to produce pyruvate and glutamate. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt the conversion of alanine to pyruvate |
| GO:0046686 response to cadmium ion | IEP PMID:17075075 Proteome changes in Arabidopsis thaliana roots upon exposure... | KEEP AS NON CORE | Summary: Retain the reported cadmium-responsive protein-abundance change. Reason: PMID:17075075 is a native Arabidopsis root proteome response study. The contextual expression response does not establish direct cadmium binding or a specific detoxification reaction. Supporting Evidence: |
| GO:0071456 cellular response to hypoxia | HEP PMID:31519798 Integrative Analysis from the Epigenome to Translatome Uncov... | KEEP AS NON CORE | Summary: ALAAT1 responds to low oxygen and supports subsequent recovery. Reason: PMID:17319845 documents induction and delayed alanine turnover in the mutant during reoxygenation. PMID:31519798 independently profiles the stress-response program; neither implies that ALAAT1 is universally responsible for hypoxic alanine synthesis. Supporting Evidence: file:ARATH/ALAAT1/ALAAT1-uniprot.txt Rapidly induced upon low-oxygen stress in roots and shoots. |
Loading supporting content…
Download this section (compressed HTML)Q: Does ALAAT1 have a minor cytosolic or nuclear pool in addition to the directly imaged mitochondrial pool, and can target-specific localization resolve the shared ALAAT1/ALAAT2 proteomic identification?
Experiment: Use endogenous ALAAT1 tagging with mitochondrial, nuclear and cytosolic markers and appropriate tag-position controls, together with isoform-resolving peptides where possible. Test the actual alternative pools without treating predominant mitochondrial localization as exclusion from the others.
Type: isoform-specific localization
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)