cyslabdan A

naturalproductmech:mibig-f3cb15d2b6 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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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	PSUMRJNLBIVEFF-RIVHMUOTSA-N
SMILES	C/C(=C\C[C@@H]1[C@]2(CCCC([C@@H]2C[C@@H]([C@@]1(CSC[C@@H](C(=O)O)NC(=O)C)O)O)(C)C)C)/C=C
Stereochemistry	fully defined
Cross-references	pubchem:24778014

Filing pathway

Terpenoids — 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 terpene, 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 cyslabdanicus NCBITaxon:1470456	SOURCE_ASSERTION	mibig:BGC0001910	DOI:10.1007/s10295-015-1694-6

Occurrences 3

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
Streptomyces NCBITaxon:1883	LOTUS	DOI:10.1038/JA.2008.102
Streptomyces thermocarboxydus NCBITaxon:59299	LOTUS	DOI:10.1007/S00253-019-10240-3
Streptomyces cyslabdanicus NCBITaxon:1470456	LOTUS	DOI:10.1038/JA.2016.103

Biosynthetic gene clusters 1

Accession	Host	Locus evidence	Genome
mibig:BGC0001910	Streptomyces cyslabdanicus NCBITaxon:1470456	CLUSTER_UNSTATED	genbank:LC064028.1

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	Mca amidase UniProtKB:A0A0H5B8U5		ungrounded → naturalproductmech:mibig-f3cb15d2b6	DOI:10.1007/s10295-015-1694-6

Step 1: Mca hydrolyzes the glycosylated mycothiol S-conjugate made from the CldC product in the terminal cyslabdan A step. This single-step partial pathway leaves the upstream CldA-CldD enzymatic steps and the nonenzymatic mycothiol addition uncurated.

Mechanism & Biosynthesis Overview

Causal graph — biosynthesis 3 nodes, 2 edges

Terminal Streptomyces cyslabdanicus cyslabdan A biosynthesis graph for Mca-associated hydrolysis of a mycothiol S-conjugate.

Subject	Predicate	Object	Notes	Evidence
cyslabdan mycothiol S-conjugate	is hydrolyzed by	Mca amidase	Mca is associated with hydrolysis of the mycothiol S-conjugate amide upstream of cyslabdan A formation.	DOI:10.1007/s10295-015-1694-6 https://mite.lisc.univie.ac.at/repository/MITE0000107 https://mibig.secondarymetabolites.org/repository/BGC0001910.4/index.html https://www.uniprot.org/uniprotkb/A0A0H5B8U5 https://www.ncbi.nlm.nih.gov/protein/BAR97454.1 reference DOI:10.1007/s10295-015-1694-6 evidence type PRIMARY_EXPERIMENT snippet failed to produce 1, but accumulated 4 notes Ikeda et al. number cyslabdan A as compound 1 and (7S,8S,12E)-8,17-epoxy-7-hydroxylabda-12,14-diene as compound 4. Their Streptomyces avermitilis SUKA22 mca-deletion experiment carrying the Streptomyces cyslabdanicus cld cluster showed that a mycothiol S-conjugate amidase is required downstream of nonenzymatic mycothiol addition to form cyslabdan A. reference https://mite.lisc.univie.ac.at/repository/MITE0000107 evidence type DATABASE_ASSERTION snippet Hydrolysis retrieved on 2026-10-01 notes MITE0000107 is an active Mca amidase entry for the terminal hydrolysis of the glycosylated mycothiol S-conjugate in cyslabdan A biosynthesis. It links UniProtKB:A0A0H5B8U5, GenPept BAR97454.1, MIBiG BGC0001910 and the Ikeda et al. DOI. reference https://mibig.secondarymetabolites.org/repository/BGC0001910.4/index.html evidence type DATABASE_ASSERTION snippet MITE0000107 retrieved on 2026-10-01 notes MIBiG BGC0001910.4 places BAR97454.1 inside the active Streptomyces cyslabdanicus cyslabdan A/B/C cluster as an amidase CDS and annotates the CDS with MITE0000107. reference https://www.uniprot.org/uniprotkb/A0A0H5B8U5 evidence type DATABASE_ASSERTION snippet A0A0H5B8U5_STRCP retrieved on 2026-10-01 notes Current unreviewed UniProtKB:A0A0H5B8U5 resolves as a Streptomyces cyslabdanicus 379 aa protein and cross-references EMBL LC064028 protein BAR97454.1. reference https://www.ncbi.nlm.nih.gov/protein/BAR97454.1 evidence type DATABASE_ASSERTION snippet amidase [Streptomyces cyslabdanicus] retrieved on 2026-10-01 notes GenPept BAR97454.1 is the 379 aa Streptomyces cyslabdanicus K04-0144 amidase encoded by complement(LC064028.1:10784..11923).
Mca amidase	forms	cyslabdan A	MITE records Mca hydrolysis as forming cyslabdan A.	DOI:10.1007/s10295-015-1694-6 https://mite.lisc.univie.ac.at/repository/MITE0000107 https://mibig.secondarymetabolites.org/repository/BGC0001910.4/index.html https://www.uniprot.org/uniprotkb/A0A0H5B8U5 https://www.ncbi.nlm.nih.gov/protein/BAR97454.1 reference DOI:10.1007/s10295-015-1694-6 evidence type PRIMARY_EXPERIMENT snippet failed to produce 1, but accumulated 4 notes Ikeda et al. number cyslabdan A as compound 1 and (7S,8S,12E)-8,17-epoxy-7-hydroxylabda-12,14-diene as compound 4. Their Streptomyces avermitilis SUKA22 mca-deletion experiment carrying the Streptomyces cyslabdanicus cld cluster showed that a mycothiol S-conjugate amidase is required downstream of nonenzymatic mycothiol addition to form cyslabdan A. reference https://mite.lisc.univie.ac.at/repository/MITE0000107 evidence type DATABASE_ASSERTION snippet Hydrolysis retrieved on 2026-10-01 notes MITE0000107 is an active Mca amidase entry for the terminal hydrolysis of the glycosylated mycothiol S-conjugate in cyslabdan A biosynthesis. It links UniProtKB:A0A0H5B8U5, GenPept BAR97454.1, MIBiG BGC0001910 and the Ikeda et al. DOI. reference https://mibig.secondarymetabolites.org/repository/BGC0001910.4/index.html evidence type DATABASE_ASSERTION snippet MITE0000107 retrieved on 2026-10-01 notes MIBiG BGC0001910.4 places BAR97454.1 inside the active Streptomyces cyslabdanicus cyslabdan A/B/C cluster as an amidase CDS and annotates the CDS with MITE0000107. reference https://www.uniprot.org/uniprotkb/A0A0H5B8U5 evidence type DATABASE_ASSERTION snippet A0A0H5B8U5_STRCP retrieved on 2026-10-01 notes Current unreviewed UniProtKB:A0A0H5B8U5 resolves as a Streptomyces cyslabdanicus 379 aa protein and cross-references EMBL LC064028 protein BAR97454.1. reference https://www.ncbi.nlm.nih.gov/protein/BAR97454.1 evidence type DATABASE_ASSERTION snippet amidase [Streptomyces cyslabdanicus] retrieved on 2026-10-01 notes GenPept BAR97454.1 is the 379 aa Streptomyces cyslabdanicus K04-0144 amidase encoded by complement(LC064028.1:10784..11923).

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

Explore across X-Mech

AntibioticMech (cyslabdan A) ↗ MediaIngredientMech (naturalproductmech:mibig-f3cb15d2b6) ↗ TaxonMech: Streptomyces cyslabdanicus (NCBITaxon:1470456) ↗ PathwayMech (mibig:BGC0001910) ↗

Provenance

Source concept	Source	Version
BGC0001910	MIBIG	4

This page is generated from data/natural_products/terpenoids/cyslabdan-a.yaml, which is generated from the committed inventories. Neither is edited by hand.