aspergillic acid

naturalproductmech:mibig-89037aa699 MINTED SEEDED

Grounding review: No 3-star ChEBI entry shares this structure, so the record keeps a content-hashed identifier.

What these status tags mean

Curation status describes a workflow state. SEEDED means the record entered through the source-seeding workflow; it does not imply that no later curation occurred. PROPOSED marks an addition awaiting review; REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record. These are workflow decisions, not independently verified human review. Agent-assisted contributions may appear in the record history.

Grounding describes the identifier mapping: EXACT uses an ontology identity asserted by the source; MINTED keeps a local identifier when no defensible ontology identity is available; REVIEW_NEEDED flags an exact structure whose ontology identity needs adjudication. The grounding note retains any unresolved alternatives. These tags do not establish the strength of producer or activity evidence.

Structure

Standard InChIKey	IUZCDJYHMMWBBE-UHFFFAOYSA-N
SMILES	CCC(C)C1=CN=C(C(=O)N1O)CC(C)C
Stereochemistry	undefined stereocentres — the InChIKey does not distinguish this compound from its stereoisomers
Cross-references	npatlas:NPA028490

Filing pathway

Unclassified — computed by NPClassifier npclassifier.gnps2.org@2026-09-07, which is why it is pinned rather than recomputed. The gene cluster's asserted class is nrps, other, from MIBiG.

Producer organisms 2

A claim that this taxon makes the compound. The basis says what the evidence addressed — a knockout and a database assertion are not the same claim.

Taxon	Basis	Cluster	Evidence
Aspergillus flavus NRRL3357 NCBITaxon:332952	SOURCE_ASSERTION	mibig:BGC0001516	PMID:29674152
Aspergillus flavus NCBITaxon:5059	SOURCE_ASSERTION	mibig:BGC0002602	DOI:10.3920/WMJ2018.2397

Occurrences 5

Somebody found the compound in this organism and cited it. That is not a claim that the organism makes it, and nothing here promotes one to the other.

Taxon	Source	Reference
Aspergillus subolivaceus NCBITaxon:41060	LOTUS	DOI:10.1021/JF00106A023
Aspergillus parasiticus NCBITaxon:5067	LOTUS	DOI:10.1021/JF00106A023
Aspergillus flavus NCBITaxon:5059	LOTUS	DOI:10.1016/J.FGB.2018.04.009
Aspergillus flavus NCBITaxon:5059	LOTUS	DOI:10.1016/S0021-9258(17)41131-8
Aspergillus flavus NCBITaxon:5059	LOTUS	DOI:10.3920/WMJ2018.2397

Biosynthetic gene clusters 2

Accession	Host	Locus evidence	Genome
mibig:BGC0001516	Aspergillus flavus NRRL3357 NCBITaxon:332952	CLUSTER_UNSTATED	genbank:NW_002477238.1
mibig:BGC0002602	Aspergillus flavus NCBITaxon:5059	CLUSTER_UNSTATED	genbank:MH898736.1

A locus claim and a taxon claim are different questions. Heterologous expression settles the first and leaves the second where the isolation report left it.

Mechanism & Biosynthesis Overview

Causal graph — biosynthesis 4 nodes, 3 edges

Database-asserted AsaD N-hydroxylation yielding the owner's stereochemically unspecified aspergillic acid structure. The current NRRL3357 reference is distinguished from the legacy N-terminally truncated protein. No stereoisomer, historical assay construct or stock identity is inferred. Both source clusters, their grades and the shared-structure discussion remain unchanged; not full-record sign-off.

Subject	Predicate	Object	Notes	Evidence
AsaD current NRRL3357 sequence reference	is_database_reported_catalyst_of	Database-reported AsaD N-hydroxylation	MITE and UniProt supply functional attribution; genomic deposits establish identity only. The modern assembly is not silently substituted into the owner's NW_002477238.1 or MH898736.1 cluster coordinates. No induction, knockout phenotype, membrane topology, glycosylation, heme-binding residue, physiological complex, rate or assay condition is asserted.	https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000297.json https://www.uniprot.org/uniprotkb/B8N0E9 https://www.ncbi.nlm.nih.gov/protein/QRD83397.1 https://www.ncbi.nlm.nih.gov/nuccore/CP044622.1 https://www.ncbi.nlm.nih.gov/protein/EED55032.1 https://www.ncbi.nlm.nih.gov/nuccore/EQ963473.1 reference https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000297.json evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes MITE0000297 version1, active, assigns deoxyaspergillic acid N-hydroxylation to AsaD, yielding aspergillic acid. Its knockout code is not an independently inspected experiment; the cited primary papers were inaccessible. No mutant phenotype is adopted. snippet Conversion of deoxyaspergillic acid into aspergillic acid reference https://www.uniprot.org/uniprotkb/B8N0E9 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Reviewed entry69, sequence2, 519 residues, asaD, NRRL3357/taxon332952. FUNCTION assigns oxidation of deoxyaspergillic acid to aspergillic acid. Experiment-coded annotations remain database assertions here. Current sequence updated2026-06-10; legacy EED55032.1 is explicitly flagged for erroneous initiation and an N-terminal truncation. snippet asaD oxidizes the pyrazinone reference https://www.ncbi.nlm.nih.gov/protein/QRD83397.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Complete conceptual translation and independent coded_by inspected: F9C07_2278499, A.flavus strain NRRL3357, 519 residues. The deposit uses species taxon5059 while UniProt uses strain taxon332952; the submitted strain labels are retained. reference https://www.ncbi.nlm.nih.gov/nuccore/CP044622.1 evidence type CURATOR_INFERENCE retrieved on 2026-10-07 notes Complete1560-nt/three-exon negative-strand CDS, default table1: complement(join(6272333..6273533,6273592..6273779,6273840..6274010)). Full translation equals its annotation, independent QRD83397.1 and current UniProt519aa; independent coded_by coordinates/DNA match. reference https://www.ncbi.nlm.nih.gov/protein/EED55032.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Legacy AFLA_023030 reference from A.flavus NRRL3357/taxon332952, 513 residues. It is not the full current519-residue reference. reference https://www.ncbi.nlm.nih.gov/nuccore/EQ963473.1 evidence type CURATOR_INFERENCE retrieved on 2026-10-07 notes Complete deposited1542-nt/three-exon plus-strand CDS, default table1: join(38036..38188,38249..38436,38495..39695). Translation equals independent EED55032.1 and current UniProt residues7..519. Current reference adds N-terminal MPSVPN; the remaining coding DNA matches exactly. This verifies reference sequences, not historical assay stock, transcript or construct identity.
Deoxyaspergillic acid, database-reported substrate	is_database_reported_substrate_of	Database-reported AsaD N-hydroxylation	The databases name deoxyaspergillic acid and MITE encodes the example substrate. No external substrate identifier, complete stereochemistry or upstream AsaC step is assigned.	https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000297.json https://www.uniprot.org/uniprotkb/B8N0E9 reference https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000297.json evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes MITE0000297 version1, active, assigns deoxyaspergillic acid N-hydroxylation to AsaD, yielding aspergillic acid. Its knockout code is not an independently inspected experiment; the cited primary papers were inaccessible. No mutant phenotype is adopted. reference https://www.uniprot.org/uniprotkb/B8N0E9 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Reviewed entry69, sequence2, 519 residues, asaD, NRRL3357/taxon332952. FUNCTION assigns oxidation of deoxyaspergillic acid to aspergillic acid. Experiment-coded annotations remain database assertions here. Current sequence updated2026-06-10; legacy EED55032.1 is explicitly flagged for erroneous initiation and an N-terminal truncation.
Database-reported AsaD N-hydroxylation	has_database_reported_product	Aspergillic acid, owner structure with unspecified stereo	Pinned MITE product matches owner InChIKey IUZCDJYHMMWBBE-UHFFFAOYSA-N using the repository helper and RDKit2026.03.5; both structures have stereo_complete:false. This is not a defined stereoisomer claim. No downstream AsaB step, ferric complex or pathway finality is inferred. SOURCE_ASSERTION producers, CLUSTER_UNSTATED BGC0001516/BGC0002602, occurrences and open shared-structure discussion are preserved.	https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000297.json https://www.uniprot.org/uniprotkb/B8N0E9 reference https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000297.json evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes MITE0000297 version1, active, assigns deoxyaspergillic acid N-hydroxylation to AsaD, yielding aspergillic acid. Its knockout code is not an independently inspected experiment; the cited primary papers were inaccessible. No mutant phenotype is adopted. reference https://www.uniprot.org/uniprotkb/B8N0E9 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Reviewed entry69, sequence2, 519 residues, asaD, NRRL3357/taxon332952. FUNCTION assigns oxidation of deoxyaspergillic acid to aspergillic acid. Experiment-coded annotations remain database assertions here. Current sequence updated2026-06-10; legacy EED55032.1 is explicitly flagged for erroneous initiation and an N-terminal truncation.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — biosynthesis 4 nodes, 3 edges

Separate database-reported AsaB aliphatic hydroxylation consuming the owner's stereo-unspecified aspergillic acid model. Current NRRL3357 reference B8N0E7 is distinguished from the legacy erroneous gene model. The preserved AsaD graph concerns a different N-hydroxylation step; no cross-graph reaction order, direct assay or complete stereoisomer identity is established by this addition.

Subject	Predicate	Object	Notes	Evidence
AsaB current NRRL3357 sequence reference	is_database_reported_catalyst_of	Database-reported AsaB aliphatic hydroxylation	MITE and UniProt supply functional attribution; sequence records establish current/legacy reference identity only. No purified-enzyme turnover, genetic phenotype, induction, physiological assembly, iron occupancy, metal-binding residue or assay-stock equivalence is asserted.	https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000298.json https://www.uniprot.org/uniprotkb/B8N0E7 https://www.ncbi.nlm.nih.gov/protein/QRD83399.1 https://www.ncbi.nlm.nih.gov/nuccore/CP044622.1 https://www.ncbi.nlm.nih.gov/protein/EED55030.1 https://www.ncbi.nlm.nih.gov/nuccore/EQ963473.1 reference https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000298.json evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Active MITE0000298 version1 assigns AsaB aliphatic hydroxylation of aspergillic acid to hydroxyaspergillic acid. Its knock-out code is not independently inspected genetic or biochemical evidence here. Cited primary papers were inaccessible. The listed iron cofactor does not establish measured binding or native occupancy, and the isIntermediate flag does not prove pathway finality. snippet Hydroxylation of aspergillic acid to hydroxyaspergillic acid reference https://www.uniprot.org/uniprotkb/B8N0E7 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Reviewed entry52/sequence2,298aa, asaB/AFLA_023010/F9C07_1358552, Aspergillus flavus NRRL3357/taxon332952. FUNCTION assigns conversion of aspergillic acid to hydroxyaspergillic acid. Experiment-coded annotations remain database assertions in this graph. Sequence updated2026-06-10; legacy EED55030.1 is flagged as an erroneous gene model, not an exact current sequence. reference https://www.ncbi.nlm.nih.gov/protein/QRD83399.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Complete current conceptual translation,298aa, F9C07_1358552, strain NRRL3357. Native deposit uses species taxon5059 while UniProt uses strain taxon332952; the strain labels agree. Its family product annotation alone is not compound-specific function evidence. reference https://www.ncbi.nlm.nih.gov/nuccore/CP044622.1 evidence type CURATOR_INFERENCE retrieved on 2026-10-07 notes Complete897-nt/two-exon reverse CDS complement(join(6278214..6278832,6278932..6279209)), codon1/defaulttable1. Full translation equals annotation, independent QRD83399.1 and current UniProt298aa; independent coded_by DNA/coordinates agree. Native metadata and target features read, not all unrelated chromosome annotations. reference https://www.ncbi.nlm.nih.gov/protein/EED55030.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Legacy AFLA_023010 reference,227aa, NRRL3357/taxon332952. It is not the exact current298aa reference and is not adopted as an experimentally demonstrated shorter isoform. reference https://www.ncbi.nlm.nih.gov/nuccore/EQ963473.1 evidence type CURATOR_INFERENCE retrieved on 2026-10-07 notes Complete legacy684-nt/two-exon plus CDS join(32819..33049,33362..33814), codon1/defaulttable1, equals annotation and independent EED55030.1. Current and legacy996-nt genomic spans are identical in biological orientation but CDS models differ. Protein alignment has227 identities, zero mismatches and one internal71-residue gap with two tied placements; not a measured biological deletion, transcript isoform or historical assay-construct identity.
Aspergillic acid, owner structure with unspecified stereo	is_database_example_substrate_of	Database-reported AsaB aliphatic hydroxylation	Pinned MITE reaction0/example0 substrate matches full owner InChI/key IUZCDJYHMMWBBE-UHFFFAOYSA-N with stereo_complete:false. The substrate is the owner compound rather than an added production claim. No resolved stereoisomer, AsaC step, source-coordinate replacement or producer-grade change is inferred.	https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000298.json https://www.uniprot.org/uniprotkb/B8N0E7 reference https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000298.json evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Active MITE0000298 version1 assigns AsaB aliphatic hydroxylation of aspergillic acid to hydroxyaspergillic acid. Its knock-out code is not independently inspected genetic or biochemical evidence here. Cited primary papers were inaccessible. The listed iron cofactor does not establish measured binding or native occupancy, and the isIntermediate flag does not prove pathway finality. reference https://www.uniprot.org/uniprotkb/B8N0E7 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Reviewed entry52/sequence2,298aa, asaB/AFLA_023010/F9C07_1358552, Aspergillus flavus NRRL3357/taxon332952. FUNCTION assigns conversion of aspergillic acid to hydroxyaspergillic acid. Experiment-coded annotations remain database assertions in this graph. Sequence updated2026-06-10; legacy EED55030.1 is flagged as an erroneous gene model, not an exact current sequence.
Database-reported AsaB aliphatic hydroxylation	has_database_example_product	Hydroxyaspergillic acid, database-reported product	The named encoded product remains externally ungrounded and stereochemically unspecified. No exact external stereoisomer, native iron chelate/ferriaspergillin identity, final-product claim or complete pathway is inferred. Both source clusters, SOURCE_ASSERTION producers, CLUSTER_UNSTATED grades, occurrences and open shared-structure discussion remain unchanged.	https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000298.json https://www.uniprot.org/uniprotkb/B8N0E7 reference https://github.com/mite-standard/mite_data/blob/6eacd913b2036376031072f69cbb33908f132998/mite_data/data/MITE0000298.json evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Active MITE0000298 version1 assigns AsaB aliphatic hydroxylation of aspergillic acid to hydroxyaspergillic acid. Its knock-out code is not independently inspected genetic or biochemical evidence here. Cited primary papers were inaccessible. The listed iron cofactor does not establish measured binding or native occupancy, and the isIntermediate flag does not prove pathway finality. reference https://www.uniprot.org/uniprotkb/B8N0E7 evidence type DATABASE_ASSERTION retrieved on 2026-10-07 notes Reviewed entry52/sequence2,298aa, asaB/AFLA_023010/F9C07_1358552, Aspergillus flavus NRRL3357/taxon332952. FUNCTION assigns conversion of aspergillic acid to hydroxyaspergillic acid. Experiment-coded annotations remain database assertions in this graph. Sequence updated2026-06-10; legacy EED55030.1 is flagged as an erroneous gene model, not an exact current sequence.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Explore across X-Mech

AntibioticMech (aspergillic acid) ↗ MediaIngredientMech (naturalproductmech:mibig-89037aa699) ↗ TaxonMech: Aspergillus flavus NRRL3357 (NCBITaxon:332952) ↗ TaxonMech: Aspergillus flavus (NCBITaxon:5059) ↗ PathwayMech (mibig:BGC0001516) ↗ PathwayMech (mibig:BGC0002602) ↗

Open questions 1

shared-structure — This structure is reported by more than one MIBiG entry: BGC0001516, BGC0002602. Confirm they describe the same compound rather than an upstream cross-reference error.

Provenance

Source concept	Source	Version
BGC0001516	MIBIG	5
BGC0002602	MIBIG	2

This page is generated from data/natural_products/unclassified/aspergillic-acid.yaml, which is generated from the committed inventories. Neither is edited by hand.