yA

UniProt ID: P17489
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Review Status: DRAFT
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Gene Description

yA encodes the conidial laccase (p-diphenol oxidase / hydroquinone:oxygen oxidoreductase), a copper-containing enzyme secreted into the Aspergillus nidulans conidial wall. yA catalyzes the final oxidation step converting the yellow wA-derived naphthopyrone precursor into the mature green conidial pigment; yA (yellow) mutants accumulate the yellow precursor and lack the green color.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0016491 oxidoreductase activity
IBA
GO_REF:0000033
ACCEPT
Summary: Accept: oxidoreductase activity.
Reason: Laccases are multicopper oxidases, so the general oxidoreductase parent is correct; the hydroquinone:oxygen oxidoreductase term below is the informative molecular function.
GO:0005507 copper ion binding
IEA
GO_REF:0000002
ACCEPT
Summary: Accept: copper ion binding.
Reason: The multicopper centre is essential to laccase catalysis, so copper binding here is a genuine cofactor requirement rather than an incidental metal-binding match.
GO:0005576 extracellular region
IEA
GO_REF:0000044
ACCEPT
Summary: Accept: extracellular region.
Reason: The conidial laccase acts at the spore surface after secretion, so an extracellular compartment is what the pigment-maturation step requires.
GO:0016491 oxidoreductase activity
IEA
GO_REF:0000002
ACCEPT
Summary: Accept: oxidoreductase activity.
Reason: Sequence-similarity route to the same general oxidoreductase parent as the IBA row; redundant.
GO:0042440 pigment metabolic process
IEA
GO_REF:0000117
ACCEPT
Summary: Accept: pigment metabolic process.
Reason: YA converts the WA polyketide precursor into the mature green conidial pigment, which makes pigment metabolism the correct process for this terminal step of conidial pigmentation.
GO:0052716 hydroquinone:oxygen oxidoreductase activity
IEA
GO_REF:0000120
ACCEPT
Summary: Accept: hydroquinone:oxygen oxidoreductase activity.
Reason: The laccase-level activity predicted from the multicopper oxidase domains. This is the specific molecular function, and it is independently supported by the direct enzyme assay below.
GO:0005576 extracellular region
ISS
GO_REF:0000024
ACCEPT
Summary: Accept: extracellular region.
Reason: Curator sequence-similarity assignment of the same secreted location; concordant with the electronic call.
GO:0052716 hydroquinone:oxygen oxidoreductase activity
ISS
GO_REF:0000024
ACCEPT
Summary: Accept: hydroquinone:oxygen oxidoreductase activity.
Reason: Curator sequence-similarity assignment of laccase activity; concordant with both the domain-based prediction and the direct enzyme assay.
GO:0043324 pigment metabolic process involved in developmental pigmentation
IMP
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus...
ACCEPT
Summary: Core process. yA acts in developmental conidial pigmentation.
Reason: yA is required for the developmental green pigmentation of conidia.
Supporting Evidence:
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus nidulans
GO:0048315 conidium formation
IMP
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus...
MARK AS OVER ANNOTATED
Summary: Over-annotation. yA is required for conidial pigmentation, not for conidium formation itself.
Reason: yellow-spored (yA) mutants form morphologically normal conidia that are simply the wrong colour; the phenotype is pigmentation, not formation. GO:0043324 (pigment metabolic process involved in developmental pigmentation), annotated and accepted above, captures the demonstrated role.
Supporting Evidence:
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus nidulans
GO:0052716 hydroquinone:oxygen oxidoreductase activity
IDA
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus...
ACCEPT
Summary: Core molecular function (direct). Conidial laccase (hydroquinone:oxygen oxidoreductase) activity.
Reason: Direct assay of the purified conidial laccase demonstrates the diphenol-oxidase activity.
Supporting Evidence:
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus nidulans
GO:0052716 hydroquinone:oxygen oxidoreductase activity
IMP
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus...
ACCEPT
Summary: Core molecular function. Laccase activity (mutant evidence).
Reason: yellow-spored (yA) mutants lack laccase, linking the gene to the activity.
Supporting Evidence:
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus nidulans
GO:0052716 hydroquinone:oxygen oxidoreductase activity
IDA
PMID:7000747
Developmental regulation of laccase levels in Aspergillus ni...
ACCEPT
Summary: Accept: hydroquinone:oxygen oxidoreductase activity.
Reason: Direct enzymological evidence for the developmentally regulated conidial laccase - the assay that defines YA, and the strongest row in this set.

Core Functions

Conidial laccase (copper-dependent p-diphenol oxidase): yA catalyzes the final oxidation of the wA-derived naphthopyrone precursor to the mature green conidial pigment; yA mutants are yellow.

Supporting Evidence:
  • PMID:4624671
    Absence of laccase from yellow-spored mutants of Aspergillus nidulans

References

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Notes

(yA-notes.md)

yA (Aspergillus nidulans) β€” curation notes

UniProt P17489 (LAC1_EMENI / yA). Conidial laccase (p-diphenol oxidase); structural-output tier.
- Copper laccase converting the wA-derived precursor to the mature green pigment; yellow (yA) mutants lack laccase. PMID:4624671.
- Core MF GO:0052716 hydroquinone:oxygen oxidoreductase activity (IDA). Acts downstream of the wA PKS.

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