Catalase A, the peroxisomal monofunctional heme catalase (EC 1.11.1.6) of Saccharomyces cerevisiae. Cta1 is a homotetramer that dismutates hydrogen peroxide to water and oxygen. It is imported into the peroxisomal matrix via a C-terminal PTS1 (SKF) and an internal targeting signal, where it removes H2O2 generated by fatty-acid beta-oxidation (acyl-CoA oxidase); under respiratory growth a fraction is also imported into the mitochondrial matrix. CTA1 is glucose-repressed and heme/oxygen-dependent. Its paralog Ctt1 (catalase T) is the cytosolic catalase; loss of both catalases increases oxidative protein damage.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000302 response to reactive oxygen species | IEA GO_REF:0000117 | TOO GENERAL | Summary: ARBA rule mapping catalases to response to reactive oxygen species. Catalase removes H2O2, so the term is related, but it is a response-level parent of the more precise hydrogen peroxide catabolic process. Reason: Broad stress-response term; response to hydrogen peroxide (GO:0042542), annotated here, is the more specific response term. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) |
| GO:0000302 response to reactive oxygen species | IMP PMID:15893481 Catalases protect cellular proteins from oxidative modificat... | TOO GENERAL | Summary: Lushchak & Gospodaryov 2005: a strain lacking both cytosolic and peroxisomal catalases had elevated protein carbonylation on ethanol, showing catalases protect proteins from oxidative damage. Reason: Physiological consequence of loss of H2O2 removal; response to hydrogen peroxide (GO:0042542), annotated here, is the more specific response term. Supporting Evidence: PMID:15893481 Growing in ethanol the strain deficient in cytosolic and peroxisomal catalases had 7.1-fold higher level of carbonyl proteins than that of wild-type strain. |
| GO:0004096 catalase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for catalase activity across the monofunctional heme catalase clade; Cta1 is a canonical clade member. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt SIMILARITY: Belongs to the catalase family. PMID:9931255 The structure of the peroxisomal catalase A from the budding yeast Saccharomyces cerevisiae, with 515 residues per subunit, has been determined and refined to 2.4 A resolution. |
| GO:0004096 catalase activity | IDA PMID:9931255 Structure of catalase-A from Saccharomyces cerevisiae. | ACCEPT | Summary: Mate et al. 1999 solved the catalase A structure and characterised catalatic vs peroxidatic activity of wild type and the Val111Ala variant; direct support for catalase activity. Supporting Evidence: PMID:9931255 The structure of the peroxisomal catalase A from the budding yeast Saccharomyces cerevisiae, with 515 residues per subunit, has been determined and refined to 2.4 A resolution. PMID:9931255 provide an explanation for both the increased peroxidatic activity and the reduced catalatic activity of this mutant. |
| GO:0004096 catalase activity | IEA GO_REF:0000120 | ACCEPT | Summary: ARBA/InterPro catalase domain mapping to catalase activity; correct. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt SIMILARITY: Belongs to the catalase family. |
| GO:0004096 catalase activity | IGI PMID:3897793 Isolation of the catalase A gene of Saccharomyces cerevisiae... | ACCEPT | Summary: Cohen et al. 1985 isolated cta1 mutants in a ctt1 background (with/from CTT1) lacking catalase A, and cloned CTA1 by complementation; genetic support for catalase activity of the CTA1 product. Supporting Evidence: PMID:3897793 Catalase A-deficient mutants were obtained by UV mutagenesis of a ctt1 mutant strain specifically lacking catalase T. PMID:3897793 The single recessive mutation causing specific lack of catalase A was designated cta1. |
| GO:0004096 catalase activity | IMP PMID:3897793 Isolation of the catalase A gene of Saccharomyces cerevisiae... | ACCEPT | Summary: cta1 mutants specifically lack catalase A activity; supports catalase activity. Supporting Evidence: PMID:3897793 The single recessive mutation causing specific lack of catalase A was designated cta1. |
| GO:0004096 catalase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways superoxide radicals degradation (DETOX1-PWY) assigns Cta1 the 2 H2O2 -> 2 H2O + O2 step (EC 1.11.1.6); correct. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) |
| GO:0005515 protein binding | IPI PMID:16606443 Comparative analysis of Saccharomyces cerevisiae WW domains ... | REMOVE | Summary: High-throughput screen of WW-domain interactors (Hesselberth et al. 2006) detected Cta1 binding to the Rsp5 ubiquitin ligase. Generic protein binding carries no functional information and no functional consequence for catalase was shown; removal does not imply the interaction is false. Reason: Uninformative generic protein binding term from a high-throughput interaction screen. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt P15202; P39940: RSP5; NbExp=2; IntAct=EBI-4061, EBI-16219; |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA for cytoplasm across catalases. Cta1 resides in the peroxisomal matrix (and mitochondrial matrix under respiratory growth), which GO places within the cytoplasm, so the term is not wrong; but the cytoplasmic catalase in yeast is the paralog Ctt1. Reason: True only by containment (peroxisome is part of the cytoplasm); the informative locations are peroxisomal and mitochondrial matrix. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000157252 · PTN000157252 SUPPORTS TRANSFER Catalases are cytoplasmic in the broad sense; Cta1 is specifically organellar. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt SUBCELLULAR LOCATION: Peroxisome matrix file:yeast/CTA1/CTA1-uniprot.txt is catalase T, which is the cytoplasmic form. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA for mitochondrion seeded by CTA1 itself (SGD:S000002664) at PTN000157252; reflects the experimental dual targeting of catalase A to mitochondria. Reason: Mitochondrial import is condition-dependent (respiratory growth); peroxisome is the principal location. Supporting Evidence: PMID:14998369 catalase A was efficiently targeted to the mitochondrial matrix where it presumably functions as scavenger of H2O2 and mitochondrial-derived ROS. |
| GO:0005759 mitochondrial matrix | IDA PMID:14998369 Dual targeting of yeast catalase A to peroxisomes and mitoch... | ACCEPT | Summary: Petrova et al. 2004 showed by fractionation, Western blotting, activity assays and GFP imaging that Cta1 is imported into the mitochondrial matrix under respiratory growth (raffinose), despite lacking a classical presequence. Supporting Evidence: PMID:14998369 catalase A was efficiently targeted to the mitochondrial matrix where it presumably functions as scavenger of H2O2 and mitochondrial-derived ROS. |
| GO:0005777 peroxisome | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for peroxisome from catalases of animals and yeast (incl. CTA1); correct, Cta1 carries PTS1 (C-terminal SKF) and an internal targeting signal. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt SUBCELLULAR LOCATION: Peroxisome matrix PMID:14998369 Efficient Cta1p import into peroxisomes was observed when cells were cultivated under peroxisome-inducing conditions (i.e. growth on oleate) |
| GO:0005782 peroxisomal matrix | IDA PMID:1986244 Peroxisomes in Saccharomyces cerevisiae: immunofluorescence ... | ACCEPT | Summary: Thieringer et al. 1991 imported catalase A into isolated peroxisomes in a protease-protected manner; UniProt cites this for peroxisome matrix. Supporting Evidence: PMID:1986244 A concentrated peroxisomal fraction was used for in vitro import of catalase A. file:yeast/CTA1/CTA1-uniprot.txt SUBCELLULAR LOCATION: Peroxisome matrix |
| GO:0005782 peroxisomal matrix | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping (SL-0202 Peroxisome matrix); correct. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt SUBCELLULAR LOCATION: Peroxisome matrix |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways DETOX1-PWY places the catalase reaction in the cytosol for both catalases. Cta1 is imported into peroxisomes (and mitochondria); the cytosolic catalase is the paralog Ctt1. Reason: Pathway-default compartment contradicted by the experimentally established peroxisomal/mitochondrial matrix location of Cta1. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt SUBCELLULAR LOCATION: Peroxisome matrix file:yeast/CTA1/CTA1-uniprot.txt is catalase T, which is the cytoplasmic form. PMID:14998369 Efficient Cta1p import into peroxisomes was observed when cells were cultivated under peroxisome-inducing conditions (i.e. growth on oleate) |
| GO:0006979 response to oxidative stress | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro catalase signature mapping to response to oxidative stress; related but a broad response term. Reason: Broad response term; response to hydrogen peroxide (GO:0042542), annotated here, is the more specific response term. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) |
| GO:0019430 removal of superoxide radicals | RCA GO_REF:0000123 | REMOVE | Summary: Inherited from the YeastPathways superoxide radicals degradation pathway (DETOX1-PWY). Catalase does not remove superoxide; it degrades the H2O2 produced by superoxide dismutase. Reason: GO:0019430 removal of superoxide radicals describes conversion of superoxide (O2-), e.g. by superoxide dismutase. Catalase acts on hydrogen peroxide, the product of SOD, and does not react with superoxide. The row is inherited from the YeastPathways "superoxide radicals degradation" pathway (DETOX1-PWY), whose name covers both the SOD and catalase steps; the catalase step is captured by GO:0042744 hydrogen peroxide catabolic process. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) |
| GO:0020037 heme binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA for heme binding (from human CAT); Cta1 is a heme catalase and the crystal structure shows the heme pocket. Cofactor binding. Reason: Cofactor binding underlying catalase activity. Supporting Evidence: PMID:9931255 Structural peculiarities related with the heme and NADP(H) binding pockets can be correlated with biochemical characteristics of the catalase A enzyme. |
| GO:0020037 heme binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro catalase heme-binding domain mapping; correct cofactor binding. Reason: Cofactor binding underlying catalase activity. Supporting Evidence: PMID:9931255 Structural peculiarities related with the heme and NADP(H) binding pockets can be correlated with biochemical characteristics of the catalase A enzyme. |
| GO:0042542 response to hydrogen peroxide | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA for response to hydrogen peroxide. Catalase directly destroys H2O2; the response term is a broader framing of the same role. Reason: Response-level term; H2O2 catabolic process is the direct process. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) |
| GO:0042744 hydrogen peroxide catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for hydrogen peroxide catabolic process; the direct process carried out by catalase. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) PMID:14998369 catalase A was efficiently targeted to the mitochondrial matrix where it presumably functions as scavenger of H2O2 and mitochondrial-derived ROS. |
| GO:0042744 hydrogen peroxide catabolic process | IDA PMID:9931255 Structure of catalase-A from Saccharomyces cerevisiae. | ACCEPT | Summary: Structural/biochemical characterisation of catalase A activity (H2O2 dismutation) supports H2O2 catabolism. Supporting Evidence: PMID:9931255 The structure of the peroxisomal catalase A from the budding yeast Saccharomyces cerevisiae, with 515 residues per subunit, has been determined and refined to 2.4 A resolution. PMID:9931255 provide an explanation for both the increased peroxidatic activity and the reduced catalatic activity of this mutant. |
| GO:0042744 hydrogen peroxide catabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA rule mapping catalases to hydrogen peroxide catabolic process; correct. Supporting Evidence: file:yeast/CTA1/CTA1-uniprot.txt FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) |
| GO:0042744 hydrogen peroxide catabolic process | IGI PMID:3897793 Isolation of the catalase A gene of Saccharomyces cerevisiae... | ACCEPT | Summary: Genetic analysis of cta1 in a ctt1 background (with/from CTT1) supports catalase A in H2O2 breakdown. Supporting Evidence: PMID:3897793 Catalase A-deficient mutants were obtained by UV mutagenesis of a ctt1 mutant strain specifically lacking catalase T. |
| GO:0042744 hydrogen peroxide catabolic process | IMP PMID:3897793 Isolation of the catalase A gene of Saccharomyces cerevisiae... | ACCEPT | Summary: cta1 mutants lacking catalase A support its role in H2O2 catabolism. Supporting Evidence: PMID:3897793 The single recessive mutation causing specific lack of catalase A was designated cta1. |
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Catalase A; breaks down hydrogen peroxide in the peroxisomal matrix formed by acyl-CoA oxidase (Pox1p) during fatty acid beta-oxidation
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