wA

UniProt ID: Q03149
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Review Status: DRAFT
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Gene Description

wA encodes the polyketide synthase responsible for the first step of conidial green-pigment biosynthesis in Aspergillus nidulans. wA produces the naphthopyrone (YWA1) precursor of the conidial pigment; wA mutants form colorless (white) conidia. The pigment is subsequently modified by downstream enzymes including the conidial laccase yA to yield the mature green color.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0016491 oxidoreductase activity
IBA
GO_REF:0000033
MARK AS OVER ANNOTATED
Summary: Imprecise MF: wA is a polyketide synthase; a generic oxidoreductase term does not capture its activity.
Reason: wA is homologous to polyketide and fatty acid synthases and performs polyketide synthesis; the IBA 'oxidoreductase activity' is an imprecise propagation.
Proposed replacements: polyketide synthase activity
GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
IEA
GO_REF:0000002
ACCEPT
Summary: Accept: 3-oxoacyl-[acyl-carrier-protein] synthase activity.
Reason: The ketosynthase domain of the WA polyketide synthase. The term names the condensation step of polyketide chain extension, which is the catalytic core of the megasynthase.
GO:0006633 fatty acid biosynthetic process
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: Over-annotated: wA makes a polyketide pigment, not fatty acids.
Reason: Propagated from fatty-acid-synthase homology; wA synthesizes the naphthopyrone pigment precursor, not fatty acids.
Proposed replacements: pigment biosynthetic process
GO:0016740 transferase activity
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: Generic transferase-activity term.
Reason: Root-level electronic term; uninformative for the PKS.
GO:0016746 acyltransferase activity
IEA
GO_REF:0000002
ACCEPT
Summary: Accept: acyltransferase activity.
Reason: The acyltransferase domain that loads extender units onto the carrier protein; a constituent activity of the same megasynthase rather than an independent function.
GO:0031177 phosphopantetheine binding
IEA
GO_REF:0000002
ACCEPT
Summary: Accept: phosphopantetheine binding.
Reason: The phosphopantetheine attachment site of the acyl-carrier domain. A cofactor/structural facet of the WA polyketide synthase, not a separate biological role.
GO:0046148 pigment biosynthetic process
IEA
GO_REF:0000117
ACCEPT
Summary: Accept: pigment biosynthetic process.
Reason: WA produces the polyketide precursor of the conidial green pigment, so a pigment-biosynthesis process term is correct; the developmental-pigmentation term below is the more specific statement.
GO:0019748 secondary metabolic process
NAS
PMID:22228366
Advances in Aspergillus secondary metabolite research in the...
ACCEPT
Summary: Accept: secondary metabolic process.
Reason: Author statement in a review of Aspergillus secondary metabolism. Correct in that a polyketide product is a secondary metabolite, but NAS from a review article is the weakest evidence line here and the term is very general.
GO:0052716 hydroquinone:oxygen oxidoreductase activity
IMP
PMID:7050088
Purification and characterization of the conidial laccase of...
REMOVE
Summary: Mis-attributed: laccase (hydroquinone:oxygen oxidoreductase) activity is that of the conidial laccase yA, not the PKS wA, and is contradicted by the cited paper itself.
Reason: The cited paper (PMID:7050088) purifies the conidial laccase and states that laccase activity is absent "in a strain carrying a mutation in the structural gene for laccase" (yA), and that wA strains lack the laccase's substrate (the wA-derived pigment precursor) - i.e. wA supplies the substrate and is upstream of the laccase, it is not the laccase. Combined with wA being a polyketide synthase (PMID:1465094), the GO:0052716 activity is a wrong-enzyme cross-attribution to wA, not merely an over-broad annotation. This is a genuinely contradicted molecular function (the cited evidence refutes it), so REMOVE rather than MARK_AS_OVER_ANNOTATED.
Supporting Evidence:
PMID:7050088
Since wA strains lack the precursor of the wild-type green pigment, i.e., the laccase substrate
GO:0043324 pigment metabolic process involved in developmental pigmentation
IMP
PMID:4624671
Absence of laccase from yellow-spored mutants of Aspergillus...
ACCEPT
Summary: Accept: pigment metabolic process involved in developmental pigmentation.
Reason: The most informative process term in this set: the classic spore-colour mutant series ties the WA polyketide product specifically to conidial pigmentation rather than to secondary metabolism at large.
GO:0046148 pigment biosynthetic process
IMP
PMID:1465094
The developmentally regulated Aspergillus nidulans wA gene e...
ACCEPT
Summary: Core process. wA is required for conidial pigment biosynthesis.
Reason: wA is required for green-pigment synthesis; wA mutants have white conidia.
Supporting Evidence:
PMID:1465094
The Aspergillus nidulans wA gene is required for synthesis of a green pigment present in the walls of mature asexual spores (conidia); wA mutants produce colorless (white) conidia

Core Functions

Polyketide synthase for conidial pigment biosynthesis: wA synthesizes the naphthopyrone (YWA1) precursor of the green conidial pigment; downstream enzymes (including the laccase yA) convert it to the mature pigment. wA mutants produce white conidia.

Supporting Evidence:
  • PMID:1465094
    The Aspergillus nidulans wA gene is required for synthesis of a green pigment present in the walls of mature asexual spores (conidia); wA mutants produce colorless (white) conidia.
  • PMID:1465094
    It is therefore likely that wA encodes all or part of a polyketide synthase involved in the formation of this pigment
  • PMID:1465094
    The Aspergillus nidulans wA gene is required for synthesis of a green pigment present in the walls of mature asexual spores (conidia); wA mutants produce colorless (white) conidia

References

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Notes

(wA-notes.md)

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