fum1 (SPCC18.18c; UniProt O94552) encodes class II fumarate hydratase (fumarase; EC 4.2.1.2), which hydrates fumarate to L-malate in the mitochondrial TCA cycle. By similarity to S. cerevisiae and human fumarase, a single gene may make both mitochondrial and extramitochondrial forms, and the cytosolic/nuclear pool may help the DNA damage response, but none of this has been shown in S. pombe.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: Generic InterPro-derived parent of the specific activity, which is already annotated. Reason: Too general. Proposed replacements: fumarate hydratase activity Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O; |
| GO:0004333 fumarate hydratase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Fumarase activity (PAINT/EC/similarity). Reason: UniProt's curated function and catalytic-activity statements for fum1 are by similarity to S. cerevisiae fumarase FUM1 (P08417; ECO:0000250), and the protein belongs to the class-II fumarase/aspartase family, fumarase subfamily (PROSITE FUMARATE_LYASES, NCBIfam fumC_II, PANTHER PTHR11444:SF1). No S. pombe enzyme assay is cached; the activity rests on this orthology and family membership, which is strong for a conserved TCA enzyme. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Catalyzes the reversible stereospecific interconversion of fumarate to L-malate file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O file:SCHPO/fum1/fum1-uniprot.txt Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. |
| GO:0004333 fumarate hydratase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Fumarase activity (PAINT/EC/similarity). Reason: UniProt's curated function and catalytic-activity statements for fum1 are by similarity to S. cerevisiae fumarase FUM1 (P08417; ECO:0000250), and the protein belongs to the class-II fumarase/aspartase family, fumarase subfamily (PROSITE FUMARATE_LYASES, NCBIfam fumC_II, PANTHER PTHR11444:SF1). No S. pombe enzyme assay is cached; the activity rests on this orthology and family membership, which is strong for a conserved TCA enzyme. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Catalyzes the reversible stereospecific interconversion of fumarate to L-malate file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O file:SCHPO/fum1/fum1-uniprot.txt Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. |
| GO:0004333 fumarate hydratase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Fumarase activity (PAINT/EC/similarity). Reason: UniProt's curated function and catalytic-activity statements for fum1 are by similarity to S. cerevisiae fumarase FUM1 (P08417; ECO:0000250), and the protein belongs to the class-II fumarase/aspartase family, fumarase subfamily (PROSITE FUMARATE_LYASES, NCBIfam fumC_II, PANTHER PTHR11444:SF1). No S. pombe enzyme assay is cached; the activity rests on this orthology and family membership, which is strong for a conserved TCA enzyme. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Catalyzes the reversible stereospecific interconversion of fumarate to L-malate file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O file:SCHPO/fum1/fum1-uniprot.txt Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Nuclear pool by similarity to yeast and human fumarase, which relocate to the nucleus after DNA damage; not shown in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Nucleus {ECO:0000250|UniProtKB:P08417}. file:SCHPO/fum1/fum1-uniprot.txt Note=Translocates from the cytosol to the nucleus in response to DNA damage. |
| GO:0005634 nucleus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Nuclear pool by similarity to yeast and human fumarase, which relocate to the nucleus after DNA damage; not shown in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Nucleus {ECO:0000250|UniProtKB:P08417}. file:SCHPO/fum1/fum1-uniprot.txt Note=Translocates from the cytosol to the nucleus in response to DNA damage. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Cytoplasmic pool by similarity (yeast fumarase is dual-localised); not shown in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Cytoplasm {ECO:0000250|UniProtKB:P08417}. file:SCHPO/fum1/fum1-uniprot.txt Note=Translocates from the cytosol to the nucleus in response to DNA damage. |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cytoplasmic pool by similarity (yeast fumarase is dual-localised); not shown in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Cytoplasm {ECO:0000250|UniProtKB:P08417}. file:SCHPO/fum1/fum1-uniprot.txt Note=Translocates from the cytosol to the nucleus in response to DNA damage. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of mitochondrial location. Reason: Organelle claim holds: UniProt places fum1 in the mitochondrial matrix by similarity to S. cerevisiae FUM1 (P08417; ECO:0000250), and the record annotates an N-terminal mitochondrial transit peptide (residues 1-39, ECO:0000255 sequence analysis). Not shown directly in S. pombe. The matrix sub-compartment is carried separately (GO:0005759). Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix file:SCHPO/fum1/fum1-uniprot.txt TRANSIT 1..39 |
| GO:0005739 mitochondrion | ISS GO_REF:0000024 | ACCEPT | Summary: Mitochondrial location by similarity. Reason: Organelle claim holds: UniProt places fum1 in the mitochondrial matrix by similarity to S. cerevisiae FUM1 (P08417; ECO:0000250), and the record annotates an N-terminal mitochondrial transit peptide (residues 1-39, ECO:0000255 sequence analysis). Not shown directly in S. pombe. The matrix sub-compartment is carried separately (GO:0005759). Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix file:SCHPO/fum1/fum1-uniprot.txt TRANSIT 1..39 |
| GO:0005759 mitochondrial matrix | IC GO_REF:0000111 | ACCEPT | Summary: Matrix location of this TCA enzyme (inference or mapping); consistent. Reason: Two independent lines agree on the matrix: the curated subcellular location is mitochondrion matrix by similarity to S. cerevisiae FUM1 (P08417; ECO:0000250), the record has an N-terminal mitochondrial transit peptide (residues 1-39, sequence analysis), and the TCA-cycle hydration step it catalyses takes place in the matrix. Not shown directly in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix file:SCHPO/fum1/fum1-uniprot.txt TRANSIT 1..39 file:SCHPO/fum1/fum1-uniprot.txt catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: Matrix location of this TCA enzyme (inference or mapping); consistent. Reason: Two independent lines agree on the matrix: the curated subcellular location is mitochondrion matrix by similarity to S. cerevisiae FUM1 (P08417; ECO:0000250), the record has an N-terminal mitochondrial transit peptide (residues 1-39, sequence analysis), and the TCA-cycle hydration step it catalyses takes place in the matrix. Not shown directly in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix file:SCHPO/fum1/fum1-uniprot.txt TRANSIT 1..39 file:SCHPO/fum1/fum1-uniprot.txt catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle |
| GO:0005759 mitochondrial matrix | ISS GO_REF:0000024 | ACCEPT | Summary: Matrix location of this TCA enzyme (inference or mapping); consistent. Reason: Two independent lines agree on the matrix: the curated subcellular location is mitochondrion matrix by similarity to S. cerevisiae FUM1 (P08417; ECO:0000250), the record has an N-terminal mitochondrial transit peptide (residues 1-39, sequence analysis), and the TCA-cycle hydration step it catalyses takes place in the matrix. Not shown directly in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix file:SCHPO/fum1/fum1-uniprot.txt TRANSIT 1..39 file:SCHPO/fum1/fum1-uniprot.txt catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle |
| GO:0005829 cytosol | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cytosolic pool by similarity; not shown in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Cytoplasm {ECO:0000250|UniProtKB:P08417}. file:SCHPO/fum1/fum1-uniprot.txt Note=Translocates from the cytosol to the nucleus in response to DNA damage. |
| GO:0006099 tricarboxylic acid cycle | EXP PMID:37164017 Optimization of energy production and central carbon metabol... | ACCEPT | Summary: 13C tracing in S. pombe versus S. japonicus shows that S. pombe runs a respiratory, oxidative TCA cycle (curator, full text). Supporting Evidence: PMID:37164017 Here, we use two related fission yeasts, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, as a comparative model system. PMID:37164017 We show that although S. japonicus does not respire oxygen, unlike S. pombe, it is capable of efficient NADH oxidation, amino acid synthesis, and ATP generation. |
| GO:0006099 tricarboxylic acid cycle | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; TCA cycle step. Reason: UniProt's curated function and pathway statements place fum1 at the fumarate to (S)-malate step of the TCA cycle, by similarity to S. cerevisiae FUM1 (P08417; ECO:0000250); class-II fumarase family membership supports this. No S. pombe-specific fum1 mutant data is cached. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle file:SCHPO/fum1/fum1-uniprot.txt Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. file:SCHPO/fum1/fum1-uniprot.txt Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. |
| GO:0006099 tricarboxylic acid cycle | IEA GO_REF:0000120 | ACCEPT | Summary: InterPro/UniPathway mapping; consistent. Reason: UniProt's curated function and pathway statements place fum1 at the fumarate to (S)-malate step of the TCA cycle, by similarity to S. cerevisiae FUM1 (P08417; ECO:0000250); class-II fumarase family membership supports this. No S. pombe-specific fum1 mutant data is cached. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle file:SCHPO/fum1/fum1-uniprot.txt Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. file:SCHPO/fum1/fum1-uniprot.txt Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. |
| GO:0006106 fumarate metabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Fumarate metabolism; broad description of the step. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O; file:SCHPO/fum1/fum1-uniprot.txt Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. |
| GO:0006106 fumarate metabolic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Fumarate metabolism; broad description of the step. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O; file:SCHPO/fum1/fum1-uniprot.txt Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. |
| GO:0006108 malate metabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Malate metabolism; broad description of the step. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O; file:SCHPO/fum1/fum1-uniprot.txt Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. |
| GO:0006302 double-strand break repair | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Similarity transfer of a role in DSB repair (nuclear fumarase in S. cerevisiae and human cells). Not tested in S. pombe. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt In cytoplasm and nucleus, involved in DNA repair in response to DNA damage: following DNA double-strand breaks (DSBs), translocates from the cytosol to the nucleus and promotes DNA repair by catalyzing the dehydration of L-malate to fumarate. |
| GO:0006974 DNA damage response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Similarity transfer of DNA damage response; as above. Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt In cytoplasm and nucleus, involved in DNA repair in response to DNA damage: following DNA double-strand breaks (DSBs), translocates from the cytosol to the nucleus and promotes DNA repair by catalyzing the dehydration of L-malate to fumarate. file:SCHPO/fum1/fum1-uniprot.txt Note=Translocates from the cytosol to the nucleus in response to DNA damage. |
| GO:0016829 lyase activity | IEA GO_REF:0000002 | MODIFY | Summary: Generic InterPro-derived parent of the specific activity, which is already annotated. Reason: Too general. Proposed replacements: fumarate hydratase activity Supporting Evidence: file:SCHPO/fum1/fum1-uniprot.txt Reaction=(S)-malate = fumarate + H2O; |
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