Mitochondrial aspartate aminotransferase (AspAT, EC 2.6.1.1) of Saccharomyces cerevisiae, a PLP-dependent class-I aminotransferase that reversibly interconverts L-aspartate + 2-oxoglutarate and oxaloacetate + L-glutamate in the mitochondrial matrix. Under the tested nitrogen-starvation conditions, Aat1 contributes less newly synthesized aspartate than cytosolic Aat2; this comparison does not establish a universal flux ratio. Aat1 is acetylated in mitochondria and participates in metabolite exchange between mitochondria and cytosol; it is inactivated in frataxin-deficient (yfh1) cells, and its loss causes respiratory deficiency and altered iron homeostasis, consistent with a role in a malate-aspartate type NADH shuttle.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: The broad molecular-function annotation is true; the characterized or conserved L-aspartate:2-oxoglutarate transaminase activity is the informative activity. Reason: Refine to L-aspartate:2-oxoglutarate transaminase activity, already supported elsewhere in this review. This is term specificity, not a rejection of the original evidence. Proposed replacements: L-aspartate:2-oxoglutarate transaminase activity Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for aspartate transaminase activity. Aat1 is a canonical class-I aspartate aminotransferase whose catalytic residues are conserved; the family-defining activity is correctly inherited. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EC 2.6.1.1/RHEA:21824 mapping from the UniProt catalytic-activity annotation; correct for Aat1. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | ISA PMID:1482685 AAT1, a gene encoding a mitochondrial aspartate aminotransfe... | ACCEPT | Summary: Sequence-alignment inference from the cytosolic paralogue Aat2 (P23542) in the AAT1 cloning paper; the paper showed conservation of catalytically important regions. Consistent with the AspAT activity of Aat1. Supporting Evidence: PMID:1482685 Sequence comparison of this yeast AspAT with AspATs from other organisms shows a high degree of homology in regions previously shown to be important for catalysis. PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | ISS GO_REF:0000024 | ACCEPT | Summary: ISS from mammalian mitochondrial AspAT (P00508, chicken GOT2). Aat1 is the yeast mitochondrial AspAT orthologue; activity is conserved. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (ASPARAGINE-BIOSYNTHESIS-1 (L-asparagine biosynthesis I)) asserting aspartate transaminase activity for Aat1. The asparagine pathway merely draws on aspartate; the activity itself is correct. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (ASPARAGINE-DEG2-PWY (asparagine degradation)) asserting aspartate transaminase activity for Aat1. The asparagine degradation pathway uses AspAT to deaminate the aspartate released by asparaginase; the activity itself is correct. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (ASPARTATESYN-PWY (L-aspartate biosynthesis)) asserting aspartate transaminase activity for Aat1. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (ASPBIO-PWY (L-aspartate biosynthesis)) asserting aspartate transaminase activity for Aat1. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (P4-PWY-1 (superpathway of lysine, threonine and methionine biosynthesis)) asserting aspartate transaminase activity for Aat1. The superpathway context is broad, but the activity assertion is correct. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (PWY3O-7 (L-homoserine biosynthesis)) asserting aspartate transaminase activity for Aat1. YeastCyc starts the homoserine pathway at oxaloacetate; the activity itself is correct. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0004069 L-aspartate:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (THRESYN-PWY (superpathway of L-threonine biosynthesis)) asserting aspartate transaminase activity for Aat1. YeastCyc starts the threonine superpathway at oxaloacetate; the activity itself is correct. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0005739 mitochondrion | HDA PMID:14576278 The proteome of Saccharomyces cerevisiae mitochondria. | ACCEPT | Summary: Retain the supported mitochondrial localization alongside the existing matrix annotation. Reason: Highly purified yeast mitochondria were analyzed by tandem mass spectrometry in PMID:14576278. Together with curated Aat1 matrix localization, this supports the organelle claim without turning whole-organelle proteomics into a matrix-resolved assay. Retain the informative mitochondrion assertion under the root-organelle policy; existing mitochondrial matrix annotations are separate and are not substituted for this row. Supporting Evidence: PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: Retain the supported mitochondrial localization alongside the existing matrix annotation. Reason: The PROMITO proteomics study (PMID:16823961) supports the original mitochondrial assignment. Together with curated Aat1 matrix localization, this supports the organelle claim without turning whole-organelle proteomics into a matrix-resolved assay. Retain the informative mitochondrion assertion under the root-organelle policy; existing mitochondrial matrix annotations are separate and are not substituted for this row. Supporting Evidence: PMID:16823961 A total of 851 different proteins (PROMITO dataset) were identified file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | ACCEPT | Summary: Retain the supported mitochondrial localization alongside the existing matrix annotation. Reason: PMID:24769239 studies isolated yeast mitochondrial proteomes under different carbon-source conditions. Together with curated Aat1 matrix localization, this supports the organelle claim without turning whole-organelle proteomics into a matrix-resolved assay. Retain the informative mitochondrion assertion under the root-organelle policy; existing mitochondrial matrix annotations are separate and are not substituted for this row. Supporting Evidence: PMID:24769239 we performed an overall quantitative proteomic and phosphoproteomic study of isolated mitochondria file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: Retain the supported mitochondrial localization alongside the existing matrix annotation. Reason: The inherited mitochondrial claim is independently supported by native yeast mitochondrial proteomics (PMID:14576278) and curated Aat1 matrix localization. The recorded PANTHER:PTN000222845 provenance does not identify a biological transfer failure; the organelle term is informative even alongside matrix annotation. Retain the informative mitochondrion assertion under the root-organelle policy; existing mitochondrial matrix annotations are separate and are not substituted for this row. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005739 mitochondrion | IDA PMID:22010850 Inactivation of mitochondrial aspartate aminotransferase con... | ACCEPT | Summary: Retain the supported mitochondrial localization alongside the existing matrix annotation. Reason: PMID:22010850 directly examines Aat1 acetylation and enzymatic inactivation in yeast mitochondria. The native mitochondrial enzyme pool supports the organelle annotation; a matrix-specific assertion is not required to preserve this result. Retain the informative mitochondrion assertion under the root-organelle policy; existing mitochondrial matrix annotations are separate and are not substituted for this row. Supporting Evidence: PMID:22010850 complete inactivation of the mitochondrial aspartate aminotransferase (Aat1) PMID:22010850 Aat1 is acetylated in wild-type mitochondria |
| GO:0005739 mitochondrion | ISS GO_REF:0000024 | ACCEPT | Summary: Retain the supported mitochondrial localization alongside the existing matrix annotation. Reason: The similarity-based mitochondrial claim is independently corroborated by native yeast mitochondrial proteomics (PMID:14576278) and curated Aat1 matrix localization. There is no target-specific evidence of lost mitochondrial localization. Retain the informative mitochondrion assertion under the root-organelle policy; existing mitochondrial matrix annotations are separate and are not substituted for this row. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping (SL-0170, mitochondrion matrix), based on Huh et al. and mitochondrial proteomics; the mitochondrial AspAT is a matrix enzyme. Most precise location. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA (ASPARAGINE-BIOSYNTHESIS-1 (L-asparagine biosynthesis I)) placing the AspAT reaction in the cytosol and attaching both isozymes. Aat1 is the mitochondrial (matrix) isozyme; the cytosolic reaction belongs to Aat2. Reason: Wrong compartment for this isozyme; YeastCyc assigns the cytosolic reaction to both Aat1 and Aat2 without compartment discrimination. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA (ASPARAGINE-DEG2-PWY (asparagine degradation)) placing the AspAT reaction in the cytosol and attaching both isozymes. Aat1 is the mitochondrial (matrix) isozyme; the cytosolic reaction belongs to Aat2. Reason: Wrong compartment for this isozyme; YeastCyc assigns the cytosolic reaction to both Aat1 and Aat2 without compartment discrimination. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA (ASPARTATESYN-PWY (L-aspartate biosynthesis)) placing the AspAT reaction in the cytosol and attaching both isozymes. Aat1 is the mitochondrial (matrix) isozyme; the cytosolic reaction belongs to Aat2. Reason: Wrong compartment for this isozyme; YeastCyc assigns the cytosolic reaction to both Aat1 and Aat2 without compartment discrimination. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA (ASPBIO-PWY (L-aspartate biosynthesis)) placing the AspAT reaction in the cytosol and attaching both isozymes. Aat1 is the mitochondrial (matrix) isozyme; the cytosolic reaction belongs to Aat2. Reason: Wrong compartment for this isozyme; YeastCyc assigns the cytosolic reaction to both Aat1 and Aat2 without compartment discrimination. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA (P4-PWY-1 (superpathway of lysine, threonine and methionine biosynthesis)) placing the AspAT reaction in the cytosol and attaching both isozymes. Aat1 is the mitochondrial (matrix) isozyme; the cytosolic reaction belongs to Aat2. Reason: Wrong compartment for this isozyme; YeastCyc assigns the cytosolic reaction to both Aat1 and Aat2 without compartment discrimination. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA (PWY3O-7 (L-homoserine biosynthesis)) placing the AspAT reaction in the cytosol and attaching both isozymes. Aat1 is the mitochondrial (matrix) isozyme; the cytosolic reaction belongs to Aat2. Reason: Wrong compartment for this isozyme; YeastCyc assigns the cytosolic reaction to both Aat1 and Aat2 without compartment discrimination. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA (THRESYN-PWY (superpathway of L-threonine biosynthesis)) placing the AspAT reaction in the cytosol and attaching both isozymes. Aat1 is the mitochondrial (matrix) isozyme; the cytosolic reaction belongs to Aat2. Reason: Wrong compartment for this isozyme; YeastCyc assigns the cytosolic reaction to both Aat1 and Aat2 without compartment discrimination. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix PMID:1482685 AAT1 encodes a 451 amino acid protein with a predicted molecular weight of 51,687, which is likely to be the yeast mitochondrial AspAT. PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. |
| GO:0006103 2-oxoglutarate metabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: The aminotransferase directly consumes or produces 2-oxoglutarate in its core reaction. Reason: This is participation in 2-oxoglutarate metabolism through the enzyme chemistry, not an indirect phenotype; the broad process is appropriate because the physiological direction is context dependent. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0006520 amino acid metabolic process | IEA GO_REF:0000002 | MODIFY | Summary: The enzyme directly catalyzes amino-acid metabolism; the established reaction-specific process is more informative. Reason: Retain the biological claim and refine to the supported biosynthetic or catabolic processes already represented in this review. Proposed replacements: L-aspartate biosynthetic process Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0006530 L-asparagine catabolic process | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: Aspartate transamination is the downstream carbon-skeleton conversion after asparaginase releases aspartate. Reason: An enzyme can participate in asparagine catabolism without binding asparagine itself. The reviewed pathway and reaction chemistry support a secondary role; isozyme-specific compartmental transport and quantitative flux are not established by the generic pathway import. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. PMID:36040324 Intracellular aspartate is converted to glutamate and oxaloacetate, which are easily utilised by the cell through the central nitrogen metabolism. |
| GO:0006531 aspartate metabolic process | ISS GO_REF:0000024 | MODIFY | Summary: Aspartate metabolism is correct, with more specific supported directional processes. Reason: Refine the broad process using the native biosynthetic role or the supported inherited catabolic direction; reversibility does not imply equal net flux in all conditions. Proposed replacements: L-aspartate biosynthetic process L-aspartate catabolic process Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0006531 aspartate metabolic process | RCA GO_REF:0000123 | MODIFY | Summary: Aspartate metabolism is correct, with more specific supported directional processes. Reason: Refine the broad process using the native biosynthetic role or the supported inherited catabolic direction; reversibility does not imply equal net flux in all conditions. Proposed replacements: L-aspartate biosynthetic process L-aspartate catabolic process Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0006532 L-aspartate biosynthetic process | IMP PMID:33397945 Autophagy sustains glutamate and aspartate synthesis in Sacc... | ACCEPT | Summary: aat1 deletion modestly reduced newly synthesised 13C-aspartate under nitrogen starvation (Aat2 is the major enzyme), showing Aat1 contributes to aspartate synthesis. Supporting Evidence: PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. |
| GO:0006532 L-aspartate biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (ASPBIO-PWY) for L-aspartate biosynthesis; consistent with the IMP data, although Aat1 is the minor contributor relative to Aat2. Supporting Evidence: PMID:33397945 Loss of Aat1p reduced [U-13C]-aspartate modestly, whereas synthesis of [U-13C]-aspartate was almost completely abolished in aat2Ξ cells (Fig. 6b), suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation. file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0006533 L-aspartate catabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA (PTN000222759; donors include human/rat GOT2) for aspartate catabolism. AspAT is freely reversible, and in mitochondria of other eukaryotes the enzyme participates in the malate-aspartate shuttle; in yeast Aat1 inactivation impairs this shuttle. Plausible but not the best-supported direction for yeast. Reason: Reversible reaction; direction-specific BP is a family inference. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:22010850 complete inactivation of the mitochondrial aspartate aminotransferase (Aat1) |
| GO:0006536 glutamate metabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: Glutamate is directly consumed or produced by the core transamination reaction. Reason: The enzyme performs glutamate metabolism; a generic co-substrate designation does not make this chemistry non-core. A single universal net direction is not inferred. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0006566 L-threonine metabolic process | RCA GO_REF:0000123 | MODIFY | Summary: The reviewed pathway contribution is to the biosynthetic direction through aspartate and homoserine, not to all threonine metabolism. Reason: The enzyme supplies the aspartate-forming catalytic step in the specified biosynthetic superpathway. Refine the broad metabolic term to L-threonine biosynthetic process; no threonine catabolic activity or quantitative branch flux is inferred. Proposed replacements: L-threonine biosynthetic process Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:10509015 The HOM3 gene of Saccharomyces cerevisiae encodes aspartate kinase, which catalyses the first step in the branched pathway leading to the synthesis of threonine and methionine from aspartate. |
| GO:0008483 transaminase activity | IEA GO_REF:0000002 | MODIFY | Summary: The broad molecular-function annotation is true; the characterized or conserved L-aspartate:2-oxoglutarate transaminase activity is the informative activity. Reason: Refine to L-aspartate:2-oxoglutarate transaminase activity, already supported elsewhere in this review. This is term specificity, not a rejection of the original evidence. Proposed replacements: L-aspartate:2-oxoglutarate transaminase activity Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
| GO:0009090 L-homoserine biosynthetic process | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: Aspartate formation supplies the substrate for the Hom3-Hom2-Hom6 sequence in the reviewed oxaloacetate-to-homoserine route. Reason: Retain the existing computational pathway contribution as secondary. Describing Hom3 as the first step from aspartate does not exclude the upstream aspartate-forming reaction when the pathway starts at oxaloacetate. This does not assert dedicated homoserine regulation or equal isozyme-specific flux. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:10509015 The HOM3 gene of Saccharomyces cerevisiae encodes aspartate kinase, which catalyses the first step in the branched pathway leading to the synthesis of threonine and methionine from aspartate. |
| GO:0009090 L-homoserine biosynthetic process | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: Aspartate formation supplies the substrate for the Hom3-Hom2-Hom6 sequence in the reviewed oxaloacetate-to-homoserine route. Reason: Retain the existing computational pathway contribution as secondary. Describing Hom3 as the first step from aspartate does not exclude the upstream aspartate-forming reaction when the pathway starts at oxaloacetate. This does not assert dedicated homoserine regulation or equal isozyme-specific flux. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; PMID:10509015 The HOM3 gene of Saccharomyces cerevisiae encodes aspartate kinase, which catalyses the first step in the branched pathway leading to the synthesis of threonine and methionine from aspartate. |
| GO:0030170 pyridoxal phosphate binding | IEA GO_REF:0000002 | ACCEPT | Summary: Pyridoxal phosphate binding is integral to the aminotransferase catalytic mechanism. Reason: The cofactor-binding property is core to this enzyme, not peripheral merely because it is not an independent reaction. Direct target biochemical evidence, where available, and conserved PLP-dependent architecture support the claim. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; file:yeast/AAT1/AAT1-uniprot.txt SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent |
| GO:0070981 L-asparagine biosynthetic process | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: Aspartate formation is the immediate substrate-supplying reaction in the represented AspAT-to-asparagine-synthetase route. Reason: Retain the reviewed pathway contribution as secondary to aspartate synthesis; AspAT does not perform amidation, and this annotation does not establish equal Aat1/Aat2 flux or every downstream amino-acid pathway. Supporting Evidence: file:yeast/AAT1/AAT1-uniprot.txt Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; |
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Download this section (compressed HTML)Q: Does Aat1 operate a malate-aspartate NADH shuttle in yeast mitochondria (exporting aspartate), and which carrier exports aspartate (Agc1)?
Q: Is Aat1 acetylation regulatory for activity in wild-type mitochondria?
Mitochondrial aspartate aminotransferase; catalyzes the conversion of oxaloacetate to aspartate in aspartate and asparagine biosynthesis
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