alo1

Summary: The PAINT mitochondrion placement is appropriate for the S. pombe fungal ALO1-family protein.

Reason: The PTHR43762 PAINT cache places a mitochondrial IBD on fungal node PTN001015900, seeded by the budding-yeast and Candida ALO1 proteins. S. pombe alo1 descends from this fungal branch, and PomBase also has target-local high-throughput localization evidence for mitochondrion, so the broad mitochondrial component is valid even though the exact fission-yeast enzymatic substrate is not established.

Summary: The InterPro membrane row is true but very broad.

Reason: The ALO_C domain is found in membrane-associated sugar-lactone oxidases, and S. pombe alo1 is already assigned to mitochondrial membrane and mitochondrial outer membrane by more informative rows. This generic membrane parent can be kept as a non-core location assertion.

Summary: The FAD lactone-oxidase InterPro mapping supports the current broad aldonolactone oxidase activity.

Reason: This InterPro row assigns the same molecular-function class that PomBase retained by IGC: an oxidoreductase acting on CH-OH donors with oxygen as acceptor. It is intentionally less specific than D-arabinono-1,4-lactone oxidase activity, which PomBase negates and current PAINT does not propagate to S. pombe alo1.

Summary: The UniProt SubCell mapping to mitochondrial membrane is consistent with the more specific PomBase outer-membrane assignment.

Reason: Mitochondrial membrane is a true but generic parent of the mitochondrial outer-membrane row transferred by PomBase from the budding-yeast ortholog. Retaining this row as non-core preserves the electronic UniProt location without overstating its precision.

Summary: alo1 carries the conserved FAD-binding domains of covalent flavoprotein oxidases.

Reason: InterPro detects the FAD-binding PCMH-type fold in Q9HDX8, and the UniProt record annotates the corresponding conserved histidyl-FAD site. FAD binding is a correct cofactor-binding assertion but subordinate to the broader oxidoreductase activity.

Summary: The PCMH-type domain supports FAD binding by alo1.

Reason: This InterPro mapping recognizes the FAD-binding PCMH domain in the protein. It is less informative than the enzyme-class annotation but is a valid cofactor-binding parent for a FAD-linked oxidoreductase.

Summary: The ORFeome localization screen places alo1 in the mitochondrion.

Reason: The cached abstract describes a fission-yeast ORFeome YFP localization resource covering roughly 90% of proteins but does not list alo1 individually. The row is retained as PomBase curator-extracted high-throughput evidence and as broad support for the ISO mitochondrial outer-membrane assignment.

Summary: PomBase transfers mitochondrial outer-membrane localization from the budding-yeast ortholog.

Reason: The SGD donor is an experimentally characterized ALO1 protein at the mitochondrial outer membrane. This orthology transfer is compatible with the broad S. pombe ORFeome mitochondrion row and with the fungal PAINT mitochondrion placement.

Summary: PomBase negates the exact budding-yeast D-arabinono-1,4-lactone oxidase activity for S. pombe alo1.

Reason: Accept this NOT row by deference to PomBase's source-specific genomic-context assertion rather than treating absent PAINT propagation as direct evidence of absence. PAINT no longer propagates exact GO:0003885 activity to S. pombe: Q9HDX8 receives only the broad PTN000356408 oxidoreductase IBA, while the exact fungal GO:0003885 assertion is placed on PTN000356435 and no longer appears in the current alo1 GOA file. The UniProt Q9HDX8 record still asserts EC 1.1.3.37 and RHEA:23756 by homology, so the visible sources conflict; the PomBase NOT row is retained as the more conservative MOD curation while the deprecated GO_REF:0000025 IGC basis is flagged for curator follow-up.

Summary: PomBase currently has no positive biological-process annotation for alo1.

Reason: The stale positive ISO to dehydro-D-arabinono-1,4-lactone biosynthesis has disappeared from the current GOA export, and PomBase now carries a NOT IGC row against that exact process. The ND biological-process root is therefore an appropriate placeholder for the absence of a known S. pombe process.

Summary: The PAINT oxidoreductase node is valid but intentionally broad for the mixed aldonolactone oxidoreductase family.

Reason: PTN000356408 sits above plant, animal, bacterial, and fungal descendants whose aldonolactone oxidoreductase substrates and products differ. PAINT correctly uses the generic GO:0016491 term at this depth; it is a safe parent activity for S. pombe alo1, but the more informative current positive activity is GO:0016899.

Summary: The ARBA activity assertion is a true but generic parent of the retained aldonolactone oxidoreductase class.

Reason: A broad oxidoreductase activity is correct for the predicted FAD-linked alo1 enzyme, but GO:0016491 is less informative than the positive GO:0016899 assertions and should not be read as evidence for a resolved D-arabinono-1,4-lactone substrate.

Summary: PomBase's genomic-context assertion captures the supported oxygen-dependent CH-OH oxidoreductase class.

Reason: PomBase retained the oxygen-dependent CH-OH oxidoreductase parent while negating the exact D-arabinono-1,4-lactone oxidase substrate. This is the best current molecular-function assertion for fission-yeast alo1: an aldonolactone oxidase-class FAD enzyme whose precise native substrate is unresolved.

Summary: PomBase negates direct transfer of the budding-yeast D-erythroascorbate biosynthetic process to S. pombe alo1.

Reason: Accept this NOT row by deference to PomBase's source-specific genomic-context assertion rather than treating absent PAINT propagation as direct evidence of absence. The old positive ISO row for this exact D-erythroascorbate process is stale and absent from the current GOA export; the current PAINT file places exact GO:0003885 activity on the narrower PTN000356435 node that S. pombe does not descend from. The PTN001015900 IRD for GO:0019853 only prunes an L-ascorbic-acid process seeded by plant, animal and bacterial donors, so it should not be read as evidence against fungal D-erythroascorbate biosynthesis. The visible GO_REF:0000025 basis for this PomBase IGC row is deprecated and operon-specific, so the negation is retained conservatively while its exact genomic-context evidence is flagged for curator follow-up.