Cao1 is a copper-dependent, quinone-containing primary amine oxidase that catalyzes oxidative deamination of primary amines. The enzyme supports utilization of ethylamine as a nitrogen source in heterologous yeast assays and obtains copper in part through the Atx1 metallochaperone. Cao1 is cytosolic in vegetative cells and concentrates within forespores during meiosis, where its activity depends on copper supplied through Mfc1.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005507 copper ion binding | IBA GO_REF:0000033 | ACCEPT | Summary: Cao1 requires bound copper for amine oxidation. Reason: Copper loading and activity assays establish the metal requirement independently of the family annotation. Supporting Evidence: PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. |
| GO:0005507 copper ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: Cao1 requires bound copper for amine oxidation. Reason: Copper loading and activity assays establish the metal requirement independently of the family annotation. Supporting Evidence: PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. |
| GO:0005737 cytoplasm | IDA PMID:18723604 Copper distributed by Atx1 is available to copper amine oxid... | MODIFY | Summary: Vegetative Cao1 is cytosolic. Reason: The target localization study and cytosolic enzyme function support the more specific soluble compartment. Proposed replacements: cytosol Supporting Evidence: PMID:18723604 Cao1-GFP was localized in the cytosol |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: Vegetative Cao1 is cytosolic. Reason: The target localization study and cytosolic enzyme function support the more specific soluble compartment. Proposed replacements: cytosol Supporting Evidence: PMID:18723604 Cao1-GFP was localized in the cytosol |
| GO:0005829 cytosol | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: Cao1 has a cytosolic vegetative localization. Reason: The target HDA assignment agrees with biochemical characterization of the soluble copper enzyme; localization changes during sporulation do not invalidate it. Supporting Evidence: PMID:18723604 Cao1-GFP was localized in the cytosol |
| GO:0006878 intracellular copper ion homeostasis | IMP PMID:18723604 Copper distributed by Atx1 is available to copper amine oxid... | KEEP AS NON CORE | Summary: Cao1 participates in intracellular copper utilization. Reason: The primary study establishes copper allocation to Cao1 by Atx1 and an Atx1-independent route. This is a contextual copper-homeostasis annotation, while Cao1’s core role is amine oxidation; copper delivery does not make Cao1 a transporter or general copper regulator. Supporting Evidence: PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. |
| GO:0008131 primary methylamine oxidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Cao1 catalyzes copper-dependent oxidative deamination of primary amines. Reason: Direct target enzyme assays establish this activity. QuickGO defines GO:0008131 by RHEA:16153 and includes primary amine oxidase as a synonym; its current label does not restrict the enzyme to methylamine alone. The meiotic paper assays Cao1 directly despite foregrounding Mfc1. Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. |
| GO:0008131 primary methylamine oxidase activity | IDA PMID:16946276 Mechanisms of copper loading on the Schizosaccharomyces pomb... | ACCEPT | Summary: Cao1 catalyzes copper-dependent oxidative deamination of primary amines. Reason: Direct target enzyme assays establish this activity. QuickGO defines GO:0008131 by RHEA:16153 and includes primary amine oxidase as a synonym; its current label does not restrict the enzyme to methylamine alone. The meiotic paper assays Cao1 directly despite foregrounding Mfc1. Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. |
| GO:0008131 primary methylamine oxidase activity | IDA PMID:18723604 Copper distributed by Atx1 is available to copper amine oxid... | ACCEPT | Summary: Cao1 catalyzes copper-dependent oxidative deamination of primary amines. Reason: Direct target enzyme assays establish this activity. QuickGO defines GO:0008131 by RHEA:16153 and includes primary amine oxidase as a synonym; its current label does not restrict the enzyme to methylamine alone. The meiotic paper assays Cao1 directly despite foregrounding Mfc1. Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. |
| GO:0008131 primary methylamine oxidase activity | IDA PMID:21828039 Mfc1 is a novel forespore membrane copper transporter in mei... | ACCEPT | Summary: Cao1 catalyzes copper-dependent oxidative deamination of primary amines. Reason: Direct target enzyme assays establish this activity. QuickGO defines GO:0008131 by RHEA:16153 and includes primary amine oxidase as a synonym; its current label does not restrict the enzyme to methylamine alone. The meiotic paper assays Cao1 directly despite foregrounding Mfc1. Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. |
| GO:0008131 primary methylamine oxidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Cao1 catalyzes copper-dependent oxidative deamination of primary amines. Reason: Direct target enzyme assays establish this activity. QuickGO defines GO:0008131 by RHEA:16153 and includes primary amine oxidase as a synonym; its current label does not restrict the enzyme to methylamine alone. The meiotic paper assays Cao1 directly despite foregrounding Mfc1. Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. PMID:18723604 the Atx1 metallochaperone represents an important source of copper for Cao1. |
| GO:0009308 amine metabolic process | IBA GO_REF:0000033 | MODIFY | Summary: Cao1 acts in amine catabolism. Reason: Oxidative deamination is degradative and the ethylamine-utilization experiment supports the catabolic child term. Proposed replacements: amine catabolic process Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. |
| GO:0009308 amine metabolic process | IEA GO_REF:0000002 | MODIFY | Summary: Cao1 acts in amine catabolism. Reason: Oxidative deamination is degradative and the ethylamine-utilization experiment supports the catabolic child term. Proposed replacements: amine catabolic process Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. |
| GO:0009310 amine catabolic process | IDA PMID:16946276 Mechanisms of copper loading on the Schizosaccharomyces pomb... | ACCEPT | Summary: Cao1 enables catabolic utilization of primary amines. Reason: Heterologous expression of fission-yeast Cao1 allows ethylamine-supported growth; this establishes enzyme capability, with the host context explicitly retained. Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. |
| GO:0042764 ascospore-type prospore | IDA PMID:21828039 Mfc1 is a novel forespore membrane copper transporter in mei... | ACCEPT | Summary: Cao1 localizes within forespores during meiosis. Reason: The full-text study images an active target Cao1-GFP fusion in a cao1 deletion background; the observation is directly about Cao1, not only the Mfc1 transporter. Supporting Evidence: PMID:21828039 Cao1-GFP displayed fluorescent staining that was mainly observed within the forespores |
| GO:0048038 quinone binding | IEA GO_REF:0000002 | ACCEPT | Summary: Cao1 uses the quinone cofactor characteristic of copper amine oxidases. Reason: The conserved copper-amine-oxidase catalytic architecture and experimentally active enzyme support its quinone cofactor; this does not imply a flavin-dependent monoamine oxidase mechanism. Supporting Evidence: file:SCHPO/cao1/cao1-uniprot.txt CC Name=L-topaquinone residue; Xref=ChEBI:CHEBI:79027; CC Evidence={ECO:0000250|UniProtKB:P46883}; |
| GO:1990748 cellular detoxification | TAS PMID:28572514 Cell-surface copper transporters and superoxide dismutase 1 ... | UNDECIDED | Summary: A detoxification role requires evidence beyond amine oxidation itself. Reason: The cited germination paper is abstract-only in the available cache and its abstract does not resolve Cao1-dependent detoxification. The established catalytic reaction can support amine use but cannot by itself establish the proposed physiological detoxification role. Supporting Evidence: PMID:16946276 Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. |
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