albonoursin

CHEBI:71609 EXACT SEEDED

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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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.

A member of the class of 2,5-diketopiperazines that is piperazine-2,5-dione in which the two hydrogen at position 3 and those at position 6 are replaced by benzylidene and isobutylidene groups (the 3Z,6Z-geoisomer).

Structure

Standard InChIKey	LCIIOYPBHIZBOD-JMVBYTIWSA-N
SMILES	CC(C)\C=C1/NC(=O)\C(NC1=O)=C\C1=CC=CC=C1
Stereochemistry	fully defined
Cross-references	npatlas:NPA016033, pubchem:6109346

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 other, from MIBiG.

Producer organisms 1

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
Streptomyces noursei ATCC 11455 NCBITaxon:316284	SOURCE_ASSERTION	mibig:BGC0000851	PMID:12498889

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
Micromonospora NCBITaxon:1873	LOTUS	DOI:10.1021/NP0104572
Streptomyces albus NCBITaxon:1888	LOTUS	DOI:10.1016/S0040-4039(01)90934-7
Streptomyces noursei NCBITaxon:1971	LOTUS	DOI:10.1080/14786419.2015.1045509
Streptomyces noursei NCBITaxon:1971	LOTUS	DOI:10.3390/MD11041035
Streptomyces albulus NCBITaxon:1971	LOTUS	DOI:10.7164/ANTIBIOTICS.52.1017

Biosynthetic gene clusters 1

Accession	Host	Locus evidence	Genome
mibig:BGC0000851	Streptomyces noursei ATCC 11455 NCBITaxon:316284	CLUSTER_DEMONSTRATED	genbank:AY129235.1

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.

Biosynthesis curated

Written by a curator with claim-level evidence on each step; not derived from a source. This is what the rest of the record exists to support.

Step	Enzyme	Reaction	Substrate → product	Evidence
1	AlbAB cyclodipeptide oxidase	RHEA:35531	CHEBI:71608 → CHEBI:71609	DOI:10.1038/s41467-024-48030-9

Step 1: AlbAB catalyzes two sequential alpha,beta-dehydrogenations of cyclo(L-phenylalanyl-L-leucyl) with O2 as the electron acceptor to form albonoursin and H2O2. This partial Streptomyces noursei ATCC 11455 pathway records the characterized CDO tailoring step and leaves AlbC-dependent cyclodipeptide precursor formation unexpanded.

Mechanism & Biosynthesis Overview

Causal graph — biosynthesis 5 nodes, 4 edges

Streptomyces noursei ATCC 11455 AlbAB-dependent alpha,beta-dehydrogenation of cyclo(L-phenylalanyl-L-leucyl) to albonoursin.

Subject	Predicate	Object	Notes	Evidence
AlbA	assembles into	AlbAB cyclodipeptide oxidase	AlbA is the FMN-bearing oxidase subunit of the AlbAB filament.	DOI:10.1038/s41467-024-48030-9 DOI:10.1016/S1074-5521(02)00285-5 https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 https://www.uniprot.org/uniprotkb/Q8GED9 https://mibig.secondarymetabolites.org/repository/BGC0000851.5/BGC0000851.gbk reference DOI:10.1038/s41467-024-48030-9 evidence type PRIMARY_EXPERIMENT snippet AlbAB showed substrate dependent enzymatic activity notes Andreas and Giessen heterologously expressed Streptomyces noursei AlbAB, purified the AlbA/AlbB filament, measured activity toward cyclo(L-Phe-L-Leu), and determined the AlbAB cryo-EM structure deposited as PDB:8UC3. reference DOI:10.1016/S1074-5521(02)00285-5 evidence type PRIMARY_EXPERIMENT snippet albA and albB, necessary for CDO activity notes Lautru et al. used purified cyclic-dipeptide oxidase peptide sequence information to clone the Streptomyces noursei albonoursin cluster, showed that the 3.8 kb fragment directs albonoursin biosynthesis in Streptomyces lividans, and demonstrated that albA and albB are both required for CDO activity. reference https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 evidence type DATABASE_ASSERTION snippet protein_id="AAN07907.1" retrieved on 2026-10-01 notes GenBank AY129235.1 maps Streptomyces noursei ATCC 11455 albA to the 711..1370 CDS and assigns protein_id AAN07907.1. reference https://www.uniprot.org/uniprotkb/Q8GED9 evidence type DATABASE_ASSERTION snippet GN=albA retrieved on 2026-10-01 notes Current Swiss-Prot UniProtKB:Q8GED9 resolves as the 219 aa Streptomyces noursei albonoursin synthase AlbA and cross-references EMBL AY129235 protein AAN07907.1. reference https://mibig.secondarymetabolites.org/repository/BGC0000851.5/BGC0000851.gbk evidence type DATABASE_ASSERTION snippet protein_id="AAN07907.1" retrieved on 2026-10-01 notes MIBiG BGC0000851.5 places albA at 711..1370 in the Streptomyces noursei albonoursin cluster and annotates the CDS as AAN07907.1 AlbA.
AlbB	assembles into	AlbAB cyclodipeptide oxidase	AlbB is required for AlbA activity and forms alternating dimers with AlbA in the active AlbAB enzyme filament.	DOI:10.1038/s41467-024-48030-9 DOI:10.1016/S1074-5521(02)00285-5 https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 https://www.uniprot.org/uniprotkb/Q8GED8 https://mibig.secondarymetabolites.org/repository/BGC0000851.5/BGC0000851.gbk reference DOI:10.1038/s41467-024-48030-9 evidence type PRIMARY_EXPERIMENT snippet AlbAB showed substrate dependent enzymatic activity notes Andreas and Giessen heterologously expressed Streptomyces noursei AlbAB, purified the AlbA/AlbB filament, measured activity toward cyclo(L-Phe-L-Leu), and determined the AlbAB cryo-EM structure deposited as PDB:8UC3. reference DOI:10.1016/S1074-5521(02)00285-5 evidence type PRIMARY_EXPERIMENT snippet albA and albB, necessary for CDO activity notes Lautru et al. used purified cyclic-dipeptide oxidase peptide sequence information to clone the Streptomyces noursei albonoursin cluster, showed that the 3.8 kb fragment directs albonoursin biosynthesis in Streptomyces lividans, and demonstrated that albA and albB are both required for CDO activity. reference https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 evidence type DATABASE_ASSERTION snippet protein_id="AAN07908.1" retrieved on 2026-10-01 notes GenBank AY129235.1 maps Streptomyces noursei ATCC 11455 albB to the overlapping 1330..1647 CDS, annotates it as required for AlbA activity, and assigns protein_id AAN07908.1. reference https://www.uniprot.org/uniprotkb/Q8GED8 evidence type DATABASE_ASSERTION snippet GN=albB retrieved on 2026-10-01 notes Current Swiss-Prot UniProtKB:Q8GED8 resolves as the 105 aa Streptomyces noursei albonoursin synthase protein AlbB and cross-references EMBL AY129235 protein AAN07908.1. reference https://mibig.secondarymetabolites.org/repository/BGC0000851.5/BGC0000851.gbk evidence type DATABASE_ASSERTION snippet protein_id="AAN07908.1" retrieved on 2026-10-01 notes MIBiG BGC0000851.5 places albB at 1330..1647 in the Streptomyces noursei albonoursin cluster and annotates the CDS as AAN07908.1 AlbB.
cyclo(L-phenylalanyl-L-leucyl)	is dehydrogenated by	AlbAB cyclodipeptide oxidase	AlbAB sequentially dehydrogenates cyclo(L-phenylalanyl-L-leucyl) to form the bis-dehydro product albonoursin.	DOI:10.1038/s41467-024-48030-9 DOI:10.1016/S1074-5521(02)00285-5 https://mite.lisc.univie.ac.at/repository/MITE0000193 https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 https://www.uniprot.org/uniprotkb/Q8GED9 https://www.uniprot.org/uniprotkb/Q8GED8 reference DOI:10.1038/s41467-024-48030-9 evidence type PRIMARY_EXPERIMENT snippet AlbAB showed substrate dependent enzymatic activity notes Andreas and Giessen heterologously expressed Streptomyces noursei AlbAB, purified the AlbA/AlbB filament, measured activity toward cyclo(L-Phe-L-Leu), and determined the AlbAB cryo-EM structure deposited as PDB:8UC3. reference DOI:10.1016/S1074-5521(02)00285-5 evidence type PRIMARY_EXPERIMENT snippet albA and albB, necessary for CDO activity notes Lautru et al. used purified cyclic-dipeptide oxidase peptide sequence information to clone the Streptomyces noursei albonoursin cluster, showed that the 3.8 kb fragment directs albonoursin biosynthesis in Streptomyces lividans, and demonstrated that albA and albB are both required for CDO activity. reference https://mite.lisc.univie.ac.at/repository/MITE0000193 evidence type DATABASE_ASSERTION snippet Dehydrogenates cyclo(L-Phe-L-Leu) retrieved on 2026-10-01 notes MITE0000193 annotates Streptomyces noursei AlbA/Q8GED9 as an active cyclic dipeptide oxidase entry, links GenPept AAN07907.1 and MIBiG BGC0000851, and maps the albonoursin dehydrogenation to RHEA:35531. reference https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 evidence type DATABASE_ASSERTION snippet protein_id="AAN07907.1" retrieved on 2026-10-01 notes GenBank AY129235.1 maps Streptomyces noursei ATCC 11455 albA to the 711..1370 CDS and assigns protein_id AAN07907.1. reference https://www.ncbi.nlm.nih.gov/nuccore/AY129235.1 evidence type DATABASE_ASSERTION snippet protein_id="AAN07908.1" retrieved on 2026-10-01 notes GenBank AY129235.1 maps Streptomyces noursei ATCC 11455 albB to the overlapping 1330..1647 CDS, annotates it as required for AlbA activity, and assigns protein_id AAN07908.1. reference https://www.uniprot.org/uniprotkb/Q8GED9 evidence type DATABASE_ASSERTION snippet GN=albA retrieved on 2026-10-01 notes Current Swiss-Prot UniProtKB:Q8GED9 resolves as the 219 aa Streptomyces noursei albonoursin synthase AlbA and cross-references EMBL AY129235 protein AAN07907.1. reference https://www.uniprot.org/uniprotkb/Q8GED8 evidence type DATABASE_ASSERTION snippet GN=albB retrieved on 2026-10-01 notes Current Swiss-Prot UniProtKB:Q8GED8 resolves as the 105 aa Streptomyces noursei albonoursin synthase protein AlbB and cross-references EMBL AY129235 protein AAN07908.1.
AlbAB cyclodipeptide oxidase	forms	albonoursin	The terminal AlbAB dehydrogenation step yields albonoursin in the BGC0000851 biosynthetic pathway.	DOI:10.1038/s41467-024-48030-9 DOI:10.1016/S1074-5521(02)00285-5 https://mite.lisc.univie.ac.at/repository/MITE0000193 reference DOI:10.1038/s41467-024-48030-9 evidence type PRIMARY_EXPERIMENT snippet AlbAB showed substrate dependent enzymatic activity notes Andreas and Giessen heterologously expressed Streptomyces noursei AlbAB, purified the AlbA/AlbB filament, measured activity toward cyclo(L-Phe-L-Leu), and determined the AlbAB cryo-EM structure deposited as PDB:8UC3. reference DOI:10.1016/S1074-5521(02)00285-5 evidence type PRIMARY_EXPERIMENT snippet albA and albB, necessary for CDO activity notes Lautru et al. used purified cyclic-dipeptide oxidase peptide sequence information to clone the Streptomyces noursei albonoursin cluster, showed that the 3.8 kb fragment directs albonoursin biosynthesis in Streptomyces lividans, and demonstrated that albA and albB are both required for CDO activity. reference https://mite.lisc.univie.ac.at/repository/MITE0000193 evidence type DATABASE_ASSERTION snippet Dehydrogenates cyclo(L-Phe-L-Leu) retrieved on 2026-10-01 notes MITE0000193 annotates Streptomyces noursei AlbA/Q8GED9 as an active cyclic dipeptide oxidase entry, links GenPept AAN07907.1 and MIBiG BGC0000851, and maps the albonoursin dehydrogenation to RHEA:35531.

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

Explore across X-Mech

AntibioticMech (albonoursin) ↗ MediaIngredientMech (CHEBI:71609) ↗ TaxonMech: Streptomyces noursei ATCC 11455 (NCBITaxon:316284) ↗ PathwayMech (mibig:BGC0000851) ↗

Provenance

Source concept	Source	Version
BGC0000851	MIBIG	5
CHEBI:71609	CHEBI	3-star

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