alo-1

UniProt ID: Q7SGY1
Organism: Neurospora crassa OR74A
Review Status: COMPLETE
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Gene Description

Neurospora crassa alo-1 encodes a membrane-associated, FAD-linked sugar-lactone oxidase in the fungal ALO1 family. By homology to characterized yeast and Candida enzymes, ALO-1 is predicted to catalyze oxidation of D-arabinono-1,4-lactone in the terminal step of fungal D-erythroascorbate biosynthesis and to act at the mitochondrial membrane, where fungal and plant ascorbate-analog oxidases are commonly localized.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003885 D-arabinono-1,4-lactone oxidase activity
IBA
GO_REF:0000033 		ACCEPT
Summary: The PANTHER PTN000356435 IBA correctly transfers the exact fungal D-arabinono-1,4-lactone oxidase activity to N. crassa ALO-1.
Reason: PTN000356435 is the ALO1-family node seeded by characterized C. albicans and S. cerevisiae ALO1 proteins. N. crassa ALO-1 is in the same PTHR43762 D-ARABINONO-1,4-LACTONE OXIDASE subfamily, retains the ALO and FAD-binding domains, and carries UniProt EC 1.1.3.37 by homology.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
PANTHER:PTN000356435 · PANTHER:PTN000356435 SUPPORTS TRANSFER
This node carries the exact EC 1.1.3.37 activity for the fungal ALO1 subfamily and is seeded by direct SGD and CGD ALO1 evidence.
Supporting Evidence:
file:interpro/panther/PTHR43762/PTHR43762-paint.tsv
PTHR43762 PTN000356435 GO:0003885 F IBD false
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
DR PANTHER; PTHR43762:SF1; D-ARABINONO-1,4-LACTONE OXIDASE; 1.
PMID:10094636
D-Arabinono-1,4-lactone oxidase catalysing the final step
PMID:11349062
We have cloned ALO1, the gene encoding D-arabinono-1,4-lactone oxidase
GO:0003885 D-arabinono-1,4-lactone oxidase activity
IEA
GO_REF:0000120 		ACCEPT
Summary: The UniProt/InterPro/Rhea electronic assertion agrees with the PAINT IBA and with the fungal ALO1 family assignment.
Reason: The exact D-arabinono-1,4-lactone oxidase activity follows from the conserved ALO_C and FAD-binding architecture, RHEA:23756/EC 1.1.3.37 mapping, and N. crassa ALO-1 membership in PANTHER subfamily PTHR43762:SF1.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
DR PANTHER; PTHR43762:SF1; D-ARABINONO-1,4-LACTONE OXIDASE; 1.
PMID:35050012
Neurospora crassa, Fusarium oxysporum, Colletotrichum gloeosporioides
GO:0005739 mitochondrion
IBA
GO_REF:0000033 		ACCEPT
Summary: The PTN001015900 IBA soundly transfers mitochondrial localization across Dikarya while avoiding over-specific membrane-side claims.
Reason: PAINT placed generic mitochondrial localization at a Dikarya node, seeded by experimentally grounded Candida and budding-yeast ALO1 annotations. N. crassa ALO-1 carries the same ALO/FAD-linked oxidoreductase domain organization, and the M. oryzae ortholog localizes to mitochondria.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
PANTHER:PTN001015900 · PANTHER:PTN001015900 SUPPORTS TRANSFER
This Dikarya ALO1 node transfers only the supported mitochondrial component rather than the narrower S. cerevisiae outer-membrane side.
Supporting Evidence:
file:interpro/panther/PTHR43762/PTHR43762-paint.tsv
PTHR43762 PTN001015900 GO:0005739 C IBD false
PMID:35050012
These data indicate that MoAlo1 is localized to the mitochondria in M. oryzae.
GO:0005739 mitochondrion
IEA
GO_REF:0000107 		ACCEPT
Summary: The Ensembl Compara transfer of broad mitochondrial localization from S. cerevisiae ALO1 is consistent with the PAINT IBA and UniProt.
Reason: Broad mitochondrial localization is the right transferable component assertion for ALO-1, unlike the narrower cytoplasmic face of the outer mitochondrial membrane.
Propagation Review
Root cause: NO FAILURE NON CORE
Sources checked:
UniProtKB:P54783 · S. cerevisiae ALO1 SUPPORTS TRANSFER
The S. cerevisiae source establishes mitochondrial localization and the broad mitochondrion component is consistent with PAINT's Dikarya-level mitochondrion IBD for fungal ALO1 proteins.
sgd:YML086C · S. cerevisiae ALO1 SUPPORTS TRANSFER
The SGD source is a valid donor for the broad mitochondrion term, while the narrower outer-membrane and cytoplasmic-side claims are treated separately below.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
PMID:35050012
These data indicate that MoAlo1 is localized to the mitochondria in M. oryzae.
GO:0005741 mitochondrial outer membrane
IEA
GO_REF:0000107 		MODIFY
Summary: The ALO-1 localization is mitochondrial membrane by homology, but the outer-membrane assignment is too specific for the available evidence.
Reason: UniProt supports only a membrane-embedded mitochondrial ALO-1 protein in N. crassa and PAINT only propagates the broader mitochondrion component. The SGD-derived outer-membrane transfer should therefore be generalized to mitochondrial membrane.
Propagation Review
Root cause: TERM SCOPING PROBLEM
Failure modes: GRANULARITY MISMATCH
Sources checked:
UniProtKB:P54783 · S. cerevisiae ALO1 SUPPORTS SOURCE BUT NOT TARGET
S. cerevisiae ALO1 is directly supported at the mitochondrial outer membrane, but N. crassa ALO-1 only has homology support for the broader mitochondrial membrane.
sgd:YML086C · S. cerevisiae ALO1 SUPPORTS SOURCE BUT NOT TARGET
The SGD donor supports outer-membrane localization in budding yeast, but transferring the same membrane specificity to N. crassa overstates the available ALO-1 evidence.
Proposed replacements: mitochondrial membrane
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
GO:0016020 membrane
IEA
GO_REF:0000002 		MODIFY
Summary: The InterPro membrane assertion is correct but less informative than the mitochondrial membrane placement in UniProt.
Reason: ALO_C domain proteins are membrane associated, and UniProt specifically places N. crassa ALO-1 at the mitochondrial membrane by homology. GO:0031966 is therefore the better component term.
Proposed replacements: mitochondrial membrane
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
CC Note=Membrane-embedded. {ECO:0000250}.
GO:0016491 oxidoreductase activity
IEA
GO_REF:0000120 		MODIFY
Summary: The ARBA/InterPro oxidoreductase call is true but too generic for an ALO1-family EC 1.1.3.37 enzyme.
Reason: N. crassa ALO-1 is specifically a D-arabinono-1,4-lactone oxidase, not only a generic oxidoreductase.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
DE EC=1.1.3.37;
GO:0016899 oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
IEA
GO_REF:0000002 		MODIFY
Summary: The lactone-oxidase InterPro mapping is directionally correct but less specific than the exact D-arabinono-1,4-lactone oxidase activity.
Reason: ALO-1 is classified into the D-arabinono-1,4-lactone oxidase subfamily and carries EC 1.1.3.37, so the exact child activity is justified.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
DE EC=1.1.3.37;
GO:0031489 myosin V binding
IEA
GO_REF:0000107 		REMOVE
Summary: The SGD-derived Myo2 binding assertion is not supported for N. crassa ALO-1.
Reason: Myosin V binding is a specific S. cerevisiae interaction claim rather than a property implied by the conserved ALO oxidase domains. No N. crassa alo-1 evidence found in this review supports this binding activity.
Propagation Review
Root cause: PROPAGATION BAD
Failure modes: LINEAGE OR TAXON MISMATCH
Sources checked:
UniProtKB:P54783 · S. cerevisiae ALO1 SUPPORTS SOURCE BUT NOT TARGET
Myo2 binding is a recent S. cerevisiae outer-membrane interaction and is not implied by ALO oxidase homology across fungi.
sgd:YML086C · S. cerevisiae ALO1 SUPPORTS SOURCE BUT NOT TARGET
The SGD source supports budding-yeast Myo2 binding, but this interaction should not be propagated to N. crassa without direct or phylogenetic evidence for conserved motor recruitment.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
RecName: Full=Putative D-arabinono-1,4-lactone oxidase
GO:0031966 mitochondrial membrane
IEA
GO_REF:0000044 		ACCEPT
Summary: UniProt's mitochondrial membrane mapping is appropriately specific for ALO-1.
Reason: N. crassa ALO-1 is predicted by homology to be membrane-embedded in the mitochondrion membrane, and fungal ALO orthologs from S. cerevisiae, C. albicans, and M. oryzae are mitochondrial or purified from mitochondrial fractions.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
PMID:10094636
purified from the mitochondrial fraction of Saccharomyces cerevisiae
PMID:7957197
purified 639-fold from the mitochondrial fraction of C. albicans
GO:0032473 cytoplasmic side of mitochondrial outer membrane
IEA
GO_REF:0000107 		MODIFY
Summary: The cytoplasmic-side outer-membrane transfer from S. cerevisiae is more specific than the localization evidence available for N. crassa ALO-1.
Reason: Homology supports a mitochondrial membrane ALO-1 protein, but neither PAINT nor the Neurospora-specific UniProt entry establishes the cytosolic face of the outer mitochondrial membrane.
Propagation Review
Root cause: TERM SCOPING PROBLEM
Failure modes: GRANULARITY MISMATCH
Sources checked:
UniProtKB:P54783 · S. cerevisiae ALO1 SUPPORTS SOURCE BUT NOT TARGET
Cytoplasmic-side mitochondrial outer-membrane localization is a budding-yeast-specific refinement not supported for N. crassa ALO-1.
sgd:YML086C · S. cerevisiae ALO1 SUPPORTS SOURCE BUT NOT TARGET
The SGD donor justifies the exact side in S. cerevisiae, whereas the N. crassa entry should be generalized to mitochondrial membrane.
Proposed replacements: mitochondrial membrane
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
GO:0034599 cellular response to oxidative stress
IEA
GO_REF:0000107 		KEEP AS NON CORE
Summary: ALO1-family enzymes supply the ascorbate analog that protects fungi from oxidative stress, but this is a physiological consequence of the biosynthetic activity rather than the core enzyme function.
Reason: S. cerevisiae, C. albicans, and M. oryzae alo1 mutants are oxidative stress sensitive, and N. crassa contains erythroascorbic acid. This supports a conserved antioxidant role while leaving D-erythroascorbate biosynthesis as the core process.
Propagation Review
Root cause: NO FAILURE NON CORE
Sources checked:
UniProtKB:P54783 · S. cerevisiae ALO1 SUPPORTS TRANSFER
Oxidative-stress sensitivity is a conserved physiological consequence of fungal D-erythroascorbate biosynthesis rather than ALO-1's core molecular activity.
sgd:YML086C · S. cerevisiae ALO1 SUPPORTS TRANSFER
The S. cerevisiae donor supports this non-core stress-response row, and N. crassa contains erythroascorbic acid.
Supporting Evidence:
PMID:10094636
The alo1 mutants showed increased sensitivity towards oxidative stress
PMID:11349062
The alo1/alo1 null mutants of C. albicans showed increased sensitivity
PMID:2825802
erythroascorbic acid were identified in extracts of the fungus Neurospora crassa
GO:0050660 flavin adenine dinucleotide binding
IEA
GO_REF:0000002 		KEEP AS NON CORE
Summary: N. crassa ALO-1 is a predicted covalent FAD flavoprotein, but FAD binding is the cofactor component of the oxidase activity.
Reason: The FAD-binding PCMH domain and His84 covalent-FAD residue support FAD binding; the informative core molecular function remains D-arabinono-1,4-lactone oxidase activity.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
FT MOD_RES 84
PMID:7957197
The enzyme showed a typical fluorescence excitation spectrum of a
GO:0070485 dehydro-D-arabinono-1,4-lactone biosynthetic process
IEA
GO_REF:0000107 		ACCEPT
Summary: ALO-1 is predicted to catalyze the final oxidase step of fungal dehydro-D-arabinono-1,4-lactone biosynthesis.
Reason: UniProt places N. crassa ALO-1 in the D-erythroascorbate biosynthesis pathway by homology; characterized S. cerevisiae and C. albicans ALO1 enzymes catalyze the same terminal step.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
UniProtKB:P54783 · S. cerevisiae ALO1 SUPPORTS TRANSFER
The donor enzyme catalyzes the same terminal D-erythroascorbate biosynthetic reaction that N. crassa ALO-1 is predicted to catalyze.
sgd:YML086C · S. cerevisiae ALO1 SUPPORTS TRANSFER
SGD's ALO1 process annotation is a sound source for the conserved fungal D-erythroascorbate biosynthesis step.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
CC -!- PATHWAY: Cofactor biosynthesis; D-erythroascorbate biosynthesis;
PMID:10094636
D-Arabinono-1,4-lactone oxidase catalysing the final step
GO:0071949 FAD binding
IEA
GO_REF:0000002 		KEEP AS NON CORE
Summary: The PCMH-domain FAD-binding mapping is sound but records a cofactor interaction of the ALO oxidase rather than a standalone core activity.
Reason: N. crassa ALO-1 has a FAD-binding PCMH-type domain and a predicted covalent FAD histidine, matching biochemically characterized Candida flavin-containing ALO.
Supporting Evidence:
file:genes/NEUCR/alo-1/alo-1-uniprot.txt
FT /note="Pros-8alpha-FAD histidine"
PMID:7957197
The flavin was not released by treatment with SDS

Core Functions

D-arabinono-1,4-lactone oxidase activity at the mitochondrial membrane, using FAD as a covalent cofactor and oxygen as electron acceptor in the final step of fungal D-erythroascorbate biosynthesis.

Molecular Function:
D-arabinono-1,4-lactone oxidase activity
Directly Involved In:
dehydro-D-arabinono-1,4-lactone biosynthetic process
Cellular Locations:
mitochondrial membrane
Supporting Evidence:
  • file:interpro/panther/PTHR43762/PTHR43762-paint.tsv
    PTHR43762 PTN000356435 GO:0003885 F IBD false
  • file:genes/NEUCR/alo-1/alo-1-uniprot.txt
    DE EC=1.1.3.37;

References

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Suggested Questions for Experts

Q: Should N. crassa ALO-1 be experimentally localized to distinguish generic mitochondrial-membrane residence from the S. cerevisiae-specific cytoplasmic side of mitochondrial outer membrane placement?

Suggested experts: Neurospora mitochondria curators, PAINT PTHR43762 curators

Suggested Experiments

Experiment: Localize ALO-1-GFP in N. crassa with mitochondrial and outer-membrane markers, and test whether alo-1 loss reduces D-erythroascorbate abundance or oxidative-stress tolerance.

📚 Additional Documentation

Notes

(alo-1-notes.md)

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