BAT1 (ECA39/TWT1) encodes the mitochondrial branched-chain amino acid aminotransferase (BCAT, EC 2.6.1.42) of Saccharomyces cerevisiae, a PLP-dependent fold-type IV transaminase imported into the mitochondrial matrix by an N-terminal presequence. Bat1 catalyses the last step in the synthesis of L-leucine, L-isoleucine and L-valine, transaminating the branched-chain 2-keto acids generated by the matrix ILV pathway with glutamate. BAT1 and its cytosolic paralog BAT2 arose from the whole-genome duplication and have subfunctionalized: BAT1 is highly expressed under biosynthetic conditions and repressed by BCAAs, whereas BAT2 carries most of the catabolic (Ehrlich pathway) transamination. bat1 bat2 double mutants are auxotrophic for Ile, Leu and Val. Bat1 can also transaminate 2-keto-4-methylthiobutyrate in methionine salvage and has been linked to TORC1 signalling and cell-cycle phenotypes, probably via metabolic effects. BAT1 was isolated as a high-copy suppressor of an atm1 mutant.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro (aminotransferase class IV) mapping to the root 'catalytic activity'. True but uninformative; Bat1 has a well-defined BCAT activity. Proposed replacements: branched-chain-amino-acid:2-oxoglutarate transaminase activity Supporting Evidence: PMID:8798704 Mitochondria and cytosol isolated from bat1 and bat2 deletion mutants, respectively, contained largely reduced activities for the conversion of branched-chain 2-ketoacids to their corresponding amino acids |
| GO:0004084 branched-chain-amino-acid:2-oxoglutarate transaminase activity | IDA PMID:8798704 Mitochondrial and cytosolic branched-chain amino acid transa... | ACCEPT | Summary: Kispal et al. showed that mitochondria from bat1-deleted cells have largely lost the conversion of the branched-chain 2-keto acids to Leu/Ile/Val, i.e. Bat1 is the mitochondrial BCAT (EC 2.6.1.42). Core MF. Supporting Evidence: PMID:8798704 Mitochondria and cytosol isolated from bat1 and bat2 deletion mutants, respectively, contained largely reduced activities for the conversion of branched-chain 2-ketoacids to their corresponding amino acids file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0004084 branched-chain-amino-acid:2-oxoglutarate transaminase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (ARBA, InterPro IPR005786 BCAT type II, EC 2.6.1.42); same as the experimentally supported core MF. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0005515 protein binding | IPI PMID:11805826 Functional organization of the yeast proteome by systematic ... | REMOVE | Summary: High-throughput affinity-purification/MS study recovering the Bat2 paralog with BAT1. Bat1 and Bat2 are 81% identical BCAT paralogs and eukaryotic BCATs are homodimers, so co-purification most plausibly reflects paralog hetero-association of tagged protein in extracts; the two proteins are normally in different compartments (matrix vs cytosol). 'protein binding' conveys no functional information and no more specific MF term (e.g. a regulatory or scaffold activity) is supported. Removal does not mean the interaction is false. Supporting Evidence: PMID:11805826 We used tandem-affinity purification (TAP) and mass spectrometry in a large-scale approach to characterize multiprotein complexes in Saccharomyces cerevisiae |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: High-throughput affinity-purification/MS study recovering the Bat2 paralog with BAT1. Bat1 and Bat2 are 81% identical BCAT paralogs and eukaryotic BCATs are homodimers, so co-purification most plausibly reflects paralog hetero-association of tagged protein in extracts; the two proteins are normally in different compartments (matrix vs cytosol). 'protein binding' conveys no functional information and no more specific MF term (e.g. a regulatory or scaffold activity) is supported. Removal does not mean the interaction is false. Supporting Evidence: PMID:16429126 Here we report the first genome-wide screen for complexes in an organism, budding yeast, using affinity purification and mass spectrometry |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: High-throughput affinity-purification/MS study recovering the Bat2 paralog with BAT1. Bat1 and Bat2 are 81% identical BCAT paralogs and eukaryotic BCATs are homodimers, so co-purification most plausibly reflects paralog hetero-association of tagged protein in extracts; the two proteins are normally in different compartments (matrix vs cytosol). 'protein binding' conveys no functional information and no more specific MF term (e.g. a regulatory or scaffold activity) is supported. Removal does not mean the interaction is false. Supporting Evidence: PMID:37968396 Here we develop a sensitive high-throughput method using highly reproducible affinity enrichment coupled to mass spectrometry |
| GO:0005737 cytoplasm | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA rule assigning 'cytoplasm', probably learned from cytosolic BCATs. Formally true because GO places the mitochondrion inside the cytoplasm, but it is uninformative and misleading for Bat1, whose location is the mitochondrial matrix (already annotated). Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: Bat1 identified in the PROMITO mass-spectrometric yeast mitochondrial proteome; consistent with its presequence-directed import. Supporting Evidence: PMID:16823961 A total of 851 different proteins (PROMITO dataset) were identified PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | ACCEPT | Summary: Bat1 found in quantitative proteomics of purified mitochondria; consistent with matrix localization. Supporting Evidence: PMID:24769239 we performed an overall quantitative proteomic and phosphoproteomic study of isolated mitochondria PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for mitochondrion in the BCAT family; Bat1 is the mitochondrial isozyme, so it is inside the clade that retained the mitochondrial location (unlike its WGD paralog Bat2). Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005759 mitochondrial matrix | EXP PMID:21267457 Saccharomyces cerevisiae Bat1 and Bat2 aminotransferases hav... | ACCEPT | Summary: ColΓ³n et al. showed Bat1-yECitrine co-localizes with MitoTracker under biosynthetic and catabolic conditions. Matrix is the established sub-compartment (presequence import). Supporting Evidence: PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005759 mitochondrial matrix | IDA PMID:8798704 Mitochondrial and cytosolic branched-chain amino acid transa... | ACCEPT | Summary: Kispal et al.: the N-terminal extension directs Bat1p to the mitochondrial matrix. Core location. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location 'Mitochondrion matrix' mapped to GO; correct. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways BRANCHED-CHAIN-AA-SYN-PWY-1 (superpathway of branched chain amino acid biosynthesis). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways ILEUSYN-PWY-1 (L-isoleucine biosynthesis I (from threonine)). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways LEUSYN-PWY-1 (L-leucine biosynthesis). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways PWY3O-351 (superpathway of methionine salvage pathway). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways PWY3O-4105 (valine degradation). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways PWY3O-4109 (isoleucine degradation). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways PWY3O-4112 (leucine degradation). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways PWY3O-64 (methionine salvage pathway). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: is_active_in cytosol from YeastPathways VALSYN-PWY (L-valine biosynthesis). YeastPathways places the BCAT reaction in the cytosol because it is shared with cytosolic Bat2; for Bat1 this is wrong: Bat1 has an N-terminal presequence and is imported into the mitochondrial matrix, where it acts on mitochondrially generated 2-keto acids. The cytosolic BCAT activity belongs to the paralog BAT2. Supporting Evidence: PMID:8798704 encodes a protein of 393 amino acid residues with an NH2-terminal extension that directs Bat1p to the mitochondrial matrix PMID:21267457 Bat1 is mitochondrially located, while Bat2 is cytoplasmic. |
| GO:0006550 L-isoleucine catabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA for isoleucine catabolism, inherited from the bifunctional ancestral BCAT. In S. cerevisiae the catabolic role was largely partitioned to Bat2 after the WGD; Bat1 contributes to catabolism only when Bat2 is absent. Not wrong, but non-core for Bat1. Supporting Evidence: PMID:21267457 These results indicate that Bat2 has a prominent role in VIL catabolism, while Bat1 catabolic role is only evidenced in a bat2Ξ genetic background |
| GO:0006550 L-isoleucine catabolic process | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: RCA from YeastPathways PWY3O-4109 (isoleucine degradation), where BAT1 is assigned the BCAT step. Bat1 can transaminate Ile in the degradative direction, but its catabolic role is only evident in bat2 mutants; the Ehrlich-pathway first step is primarily Bat2. Supporting Evidence: PMID:21267457 These results indicate that Bat2 has a prominent role in VIL catabolism, while Bat1 catabolic role is only evidenced in a bat2Ξ genetic background |
| GO:0006552 L-leucine catabolic process | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: RCA from YeastPathways PWY3O-4112 (leucine degradation), where BAT1 is assigned the BCAT step. As for isoleucine: Leu catabolism is primarily Bat2-dependent; Bat1 contribution is minor. Supporting Evidence: PMID:21267457 These results indicate that Bat2 has a prominent role in VIL catabolism, while Bat1 catabolic role is only evidenced in a bat2Ξ genetic background |
| GO:0006574 L-valine catabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA for valine catabolism from the ancestral bifunctional BCAT; for Bat1 this is a minor, back-up role (evident only in bat2 mutants). Supporting Evidence: PMID:21267457 These results indicate that Bat2 has a prominent role in VIL catabolism, while Bat1 catabolic role is only evidenced in a bat2Ξ genetic background |
| GO:0006574 L-valine catabolic process | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: RCA from YeastPathways PWY3O-4105 (valine degradation), where BAT1 is assigned the BCAT step. Val catabolism is primarily Bat2-dependent; Bat1 contribution is minor. Supporting Evidence: PMID:21267457 These results indicate that Bat2 has a prominent role in VIL catabolism, while Bat1 catabolic role is only evidenced in a bat2Ξ genetic background |
| GO:0009081 branched-chain amino acid metabolic process | IEA GO_REF:0000002 | MODIFY | Summary: InterPro mapping to the generic 'branched-chain amino acid metabolic process'. Correct but too general; Bat1's established role is the final biosynthetic transamination. Proposed replacements: branched-chain amino acid biosynthetic process Supporting Evidence: PMID:21267457 Above presented results indicate that in a wild type strain Bat1 displays a biosynthetic character while Bat2 has a prominent catabolic role. |
| GO:0009082 branched-chain amino acid biosynthetic process | IDA PMID:8798704 Mitochondrial and cytosolic branched-chain amino acid transa... | ACCEPT | Summary: Mitochondrial extracts from bat1 deletants lose 2-keto acid to amino acid conversion, the biosynthetic direction. Core BP. Supporting Evidence: PMID:8798704 Mitochondria and cytosol isolated from bat1 and bat2 deletion mutants, respectively, contained largely reduced activities for the conversion of branched-chain 2-ketoacids to their corresponding amino acids |
| GO:0009082 branched-chain amino acid biosynthetic process | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA BP assignment; consistent with the experimentally established biosynthetic role of Bat1. Supporting Evidence: PMID:21267457 Above presented results indicate that in a wild type strain Bat1 displays a biosynthetic character while Bat2 has a prominent catabolic role. |
| GO:0009082 branched-chain amino acid biosynthetic process | IMP PMID:8798704 Mitochondrial and cytosolic branched-chain amino acid transa... | ACCEPT | Summary: bat1 bat2 double deletion causes Ile/Leu/Val auxotrophy; Bat1 is the predominant biosynthetic isozyme under fermentative conditions. Supporting Evidence: PMID:8798704 deletion of both genes resulted in an auxotrophy for branched-chain amino acids (Ile, Leu, and Val) PMID:21267457 Above presented results indicate that in a wild type strain Bat1 displays a biosynthetic character while Bat2 has a prominent catabolic role. |
| GO:0009082 branched-chain amino acid biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways BRANCHED-CHAIN-AA-SYN-PWY-1 (superpathway of branched chain amino acid biosynthesis), where BAT1 is assigned the BCAT step. Correct: Bat1 catalyses the last step of Ile, Leu and Val synthesis in the matrix. Supporting Evidence: PMID:21267457 Above presented results indicate that in a wild type strain Bat1 displays a biosynthetic character while Bat2 has a prominent catabolic role. PMID:8798704 deletion of both genes resulted in an auxotrophy for branched-chain amino acids (Ile, Leu, and Val) |
| GO:0009083 branched-chain amino acid catabolic process | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA BP assignment of BCAA catabolism. True only as a minor/back-up role for Bat1 (prominent catabolic isozyme is Bat2). Supporting Evidence: PMID:21267457 These results indicate that Bat2 has a prominent role in VIL catabolism, while Bat1 catabolic role is only evidenced in a bat2Ξ genetic background |
| GO:0009083 branched-chain amino acid catabolic process | IMP PMID:8702755 Two yeast homologs of ECA39, a target for c-Myc regulation, ... | KEEP AS NON CORE | Summary: Eden et al. deleted ECA39 (=BAT1) and measured BCAT activity with Leu/Ile/Val as amino donors (the catabolic direction). The abstract does not detail the catabolic phenotype; deferring to the curator, but later work shows the catabolic role is mainly Bat2's, so non-core for Bat1. Supporting Evidence: PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates PMID:21267457 These results indicate that Bat2 has a prominent role in VIL catabolism, while Bat1 catabolic role is only evidenced in a bat2Ξ genetic background |
| GO:0009098 L-leucine biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: UniPathway mapping (L-leucine biosynthesis, step 4/4); correct for the biosynthetic Bat1 isozyme. Supporting Evidence: PMID:8798704 deletion of both genes resulted in an auxotrophy for branched-chain amino acids (Ile, Leu, and Val) |
| GO:0009098 L-leucine biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways LEUSYN-PWY-1 (L-leucine biosynthesis), where BAT1 is assigned the BCAT step. Correct: Bat1 performs the final transamination of 2-oxoisocaproate to Leu (with Bat2 as backup). Supporting Evidence: PMID:8798704 deletion of both genes resulted in an auxotrophy for branched-chain amino acids (Ile, Leu, and Val) PMID:21267457 Above presented results indicate that in a wild type strain Bat1 displays a biosynthetic character while Bat2 has a prominent catabolic role. |
| GO:0009099 L-valine biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: UniPathway mapping (L-valine biosynthesis, step 4/4); correct for Bat1. Supporting Evidence: PMID:8798704 deletion of both genes resulted in an auxotrophy for branched-chain amino acids (Ile, Leu, and Val) |
| GO:0009099 L-valine biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways VALSYN-PWY (L-valine biosynthesis), where BAT1 is assigned the BCAT step. Correct: Bat1 transaminates 2-oxoisovalerate to Val in the matrix. Supporting Evidence: PMID:8798704 deletion of both genes resulted in an auxotrophy for branched-chain amino acids (Ile, Leu, and Val) PMID:21267457 Above presented results indicate that in a wild type strain Bat1 displays a biosynthetic character while Bat2 has a prominent catabolic role. |
| GO:0010326 L-methionine:oxo-acid transaminase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: Rhea-based mapping (RHEA:31763, KMTB + amino acid -> methionine). UniProt cites Bat1 as one of the transaminases closing the methionine salvage cycle using BCAAs as amino donors. Plausible secondary activity of a broad-specificity BCAT; non-core. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage |
| GO:0052654 L-leucine:2-oxoglutarate transaminase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for L-leucine transaminase; Bat1 uses Leu/2-oxoisocaproate (Rhea:18321 in UniProt). Correct, a substrate-specific child of the core BCAT MF. Supporting Evidence: PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0052654 L-leucine:2-oxoglutarate transaminase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Rhea-based mapping (RHEA:18321); correct. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0052655 L-valine:2-oxoglutarate transaminase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for L-valine transaminase; Bat1 uses Val/2-oxoisovalerate. Correct. Supporting Evidence: PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0052655 L-valine:2-oxoglutarate transaminase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Rhea-based mapping (RHEA:24813); correct. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for L-isoleucine transaminase; correct for Bat1. Supporting Evidence: PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Rhea-based mapping (RHEA:24801); correct. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways BRANCHED-CHAIN-AA-SYN-PWY-1 (superpathway of branched chain amino acid biosynthesis). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways ILEUSYN-PWY-1 (L-isoleucine biosynthesis I (from threonine)). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways LEUSYN-PWY-1 (L-leucine biosynthesis). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Note that the source YeastPathways reaction in LEUSYN-PWY-1 is the leucine transamination, yet the YeastPathways-to-GO conversion emitted the isoleucine-specific term; this is a conversion artefact, although the statement is still true for this enzyme. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-351 (superpathway of methionine salvage pathway). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Note that the source YeastPathways reaction in PWY3O-351 is the methionine (R15-RXN, KMTB transamination) transamination, yet the YeastPathways-to-GO conversion emitted the isoleucine-specific term; this is a conversion artefact, although the statement is still true for this enzyme. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-4105 (valine degradation). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Note that the source YeastPathways reaction in PWY3O-4105 is the valine transamination, yet the YeastPathways-to-GO conversion emitted the isoleucine-specific term; this is a conversion artefact, although the statement is still true for this enzyme. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-4109 (isoleucine degradation). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-4112 (leucine degradation). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Note that the source YeastPathways reaction in PWY3O-4112 is the leucine transamination, yet the YeastPathways-to-GO conversion emitted the isoleucine-specific term; this is a conversion artefact, although the statement is still true for this enzyme. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-64 (methionine salvage pathway). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Note that the source YeastPathways reaction in PWY3O-64 is the methionine (R15-RXN, KMTB transamination) transamination, yet the YeastPathways-to-GO conversion emitted the isoleucine-specific term; this is a conversion artefact, although the statement is still true for this enzyme. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways VALSYN-PWY (L-valine biosynthesis). BAT1 transaminates L-isoleucine/2-oxoglutarate (Rhea:24801 in UniProt), so the MF is correct for this protein. Note that the source YeastPathways reaction in VALSYN-PWY is the valine transamination, yet the YeastPathways-to-GO conversion emitted the isoleucine-specific term; this is a conversion artefact, although the statement is still true for this enzyme. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial PMID:8702755 Activity of branched-chain amino acid aminotransferase was measured in the wild-type and mutants with either leucine, isoleucine, or valine as substrates |
| GO:0071267 L-methionine salvage | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: RCA from YeastPathways PWY3O-351 (superpathway of methionine salvage pathway), where BAT1 is assigned the BCAT step. UniProt (citing PMID:18625006, not cached) states Bat1 can aminate KMTB to methionine in the salvage cycle using BCAAs as donors; Aro8/Aro9 and Bat2 also contribute. A real but secondary activity of a promiscuous transaminase. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage |
| GO:0071267 L-methionine salvage | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: RCA from YeastPathways PWY3O-64 (methionine salvage pathway), where BAT1 is assigned the BCAT step. Same KMTB transamination step as the companion methionine-salvage row; secondary to BCAA biosynthesis. Supporting Evidence: file:yeast/BAT1/BAT1-uniprot.txt from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage |
| GO:1901705 L-isoleucine biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways ILEUSYN-PWY-1 (L-isoleucine biosynthesis I (from threonine)), where BAT1 is assigned the BCAT step. Correct: Bat1 catalyses the final step (step 4/4) of L-isoleucine synthesis. Supporting Evidence: PMID:8798704 deletion of both genes resulted in an auxotrophy for branched-chain amino acids (Ile, Leu, and Val) PMID:21267457 Above presented results indicate that in a wild type strain Bat1 displays a biosynthetic character while Bat2 has a prominent catabolic role. |
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Download this section (compressed HTML)Q: Is the RCA conversion of every YeastPathways BCAT reaction (Leu, Val and the methionine-salvage R15-RXN) to GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity a systematic mapping error that should be fixed at source?
Experiment: Measure 13C-leucine flux to fusel alcohols in wild type, bat1, bat2 and bat2 strains expressing presequence-less Bat1, under ammonium vs BCAA nitrogen sources.
Hypothesis: Bat1 contributes to BCAA catabolism in the matrix only when cytosolic Bat2 is absent or limiting.
Mitochondrial branched-chain amino acid (BCAA) aminotransferase; preferentially involved in BCAA biosynthesis; homolog of murine ECA39; highly expressed during logarithmic phase and repressed during stationary phase; BAT1 has a paralog, BAT2, that arose from the whole genome duplication
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