mycosporine glycine

naturalproductmech:mibig-00a364fe41 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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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	XZQILKYKJYHEHD-JTQLQIEISA-N
SMILES	O=C1C(OC)=C(NCC(O)=O)C[C@@](O)(CO)C1
Stereochemistry	fully defined

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, 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
Trichormus variabilis ATCC 29413 NCBITaxon:240292	SOURCE_ASSERTION	mibig:BGC0000427	PMID:20813918

Occurrences 4

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
Chlorogloeopsis NCBITaxon:1123	LOTUS	DOI:10.1007/S002030050759
Chlorogloeopsis NCBITaxon:1123	LOTUS	DOI:10.1016/S0742-8413(96)00135-1
Chlorogloeopsis NCBITaxon:1123	LOTUS	DOI:10.1021/JO00117A008
Chlorogloeopsis sp. NCBITaxon:28069	CYANOMETDB	PMID:26286672

Biosynthetic gene clusters 1

Accession	Host	Locus evidence	Genome
mibig:BGC0000427	Trichormus variabilis ATCC 29413 NCBITaxon:240292	CLUSTER_DEMONSTRATED	genbank:CP000117.1

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
4	Ava_3855 NRPS-like shinorine synthase UniProtKB:Q3M6C6		naturalproductmech:mibig-00a364fe41 + CHEBI:17115 → CHEBI:131712	DOI:10.1126/science.1193637

Step 4: Trichormus variabilis ATCC 29413 Ava_3855 catalyzes the ATP-dependent terminal serine incorporation step that converts mycosporine glycine to shinorine. No exact Rhea reaction was available for this serine addition.

Mechanism & Biosynthesis Overview

Causal graph — biosynthesis 4 nodes, 3 edges

Trichormus variabilis ATCC 29413 BGC0000427 NRPS-like shinorine synthase Ava_3855 couples mycosporine glycine with L-serine to form shinorine.

Subject	Predicate	Object	Notes	Evidence
mycosporine glycine	is converted to shinorine by	Ava_3855	Purified Ava_3855 uses mycosporine glycine and serine as substrates in ATP-dependent shinorine formation.	DOI:10.1126/science.1193637 https://mibig.secondarymetabolites.org/repository/BGC0000427.5/ https://www.uniprot.org/uniprotkb/Q3M6C6 reference DOI:10.1126/science.1193637 evidence type PRIMARY_EXPERIMENT snippet HPLC assays confirmed its role in converting mycosporine glycine and serine to shinorine notes Balskus and Walsh showed that the complete 6.5 kb Ava_3858-Ava_3855 cluster produced shinorine in Escherichia coli, that a construct truncated before Ava_3855 accumulated mycosporine glycine, and that purified Ava_3855 converted mycosporine glycine plus serine to shinorine in an ATP-dependent HPLC assay. reference https://mibig.secondarymetabolites.org/repository/BGC0000427.5/ evidence type DATABASE_ASSERTION retrieved on 2026-09-30 notes MIBiG entry version 5 links BGC0000427 to shinorine biosynthesis in Trichormus variabilis ATCC 29413 and lists Ava_3855 / ABA23460.1 at CP000117.1:4798900-4801566 on the minus strand. reference https://www.uniprot.org/uniprotkb/Q3M6C6 evidence type DATABASE_ASSERTION retrieved on 2026-09-30 notes Unreviewed UniProtKB:Q3M6C6 is the Trichormus variabilis ATCC 29413 / PCC 7937 Ava_3855 amino acid adenylation entry cross-referenced to EMBL CP000117 and GenPept ABA23460.1.
L-serine	is attached to mycosporine glycine by	Ava_3855	Ava_3855 activates serine through its adenylation domain and loads it onto the enzyme thiolation domain before shinorine formation.	DOI:10.1126/science.1193637 https://mibig.secondarymetabolites.org/repository/BGC0000427.5/ https://www.uniprot.org/uniprotkb/Q3M6C6 reference DOI:10.1126/science.1193637 evidence type PRIMARY_EXPERIMENT snippet HPLC assays confirmed its role in converting mycosporine glycine and serine to shinorine notes Balskus and Walsh showed that the complete 6.5 kb Ava_3858-Ava_3855 cluster produced shinorine in Escherichia coli, that a construct truncated before Ava_3855 accumulated mycosporine glycine, and that purified Ava_3855 converted mycosporine glycine plus serine to shinorine in an ATP-dependent HPLC assay. reference https://mibig.secondarymetabolites.org/repository/BGC0000427.5/ evidence type DATABASE_ASSERTION retrieved on 2026-09-30 notes MIBiG entry version 5 links BGC0000427 to shinorine biosynthesis in Trichormus variabilis ATCC 29413 and lists Ava_3855 / ABA23460.1 at CP000117.1:4798900-4801566 on the minus strand. reference https://www.uniprot.org/uniprotkb/Q3M6C6 evidence type DATABASE_ASSERTION retrieved on 2026-09-30 notes Unreviewed UniProtKB:Q3M6C6 is the Trichormus variabilis ATCC 29413 / PCC 7937 Ava_3855 amino acid adenylation entry cross-referenced to EMBL CP000117 and GenPept ABA23460.1.
Ava_3855	forms	shinorine	Full-cluster heterologous expression produced shinorine, while the Ava_3855-truncated construct accumulated mycosporine glycine.	DOI:10.1126/science.1193637 https://mibig.secondarymetabolites.org/repository/BGC0000427.5/ https://www.uniprot.org/uniprotkb/Q3M6C6 reference DOI:10.1126/science.1193637 evidence type PRIMARY_EXPERIMENT snippet HPLC assays confirmed its role in converting mycosporine glycine and serine to shinorine notes Balskus and Walsh showed that the complete 6.5 kb Ava_3858-Ava_3855 cluster produced shinorine in Escherichia coli, that a construct truncated before Ava_3855 accumulated mycosporine glycine, and that purified Ava_3855 converted mycosporine glycine plus serine to shinorine in an ATP-dependent HPLC assay. reference https://mibig.secondarymetabolites.org/repository/BGC0000427.5/ evidence type DATABASE_ASSERTION retrieved on 2026-09-30 notes MIBiG entry version 5 links BGC0000427 to shinorine biosynthesis in Trichormus variabilis ATCC 29413 and lists Ava_3855 / ABA23460.1 at CP000117.1:4798900-4801566 on the minus strand. reference https://www.uniprot.org/uniprotkb/Q3M6C6 evidence type DATABASE_ASSERTION retrieved on 2026-09-30 notes Unreviewed UniProtKB:Q3M6C6 is the Trichormus variabilis ATCC 29413 / PCC 7937 Ava_3855 amino acid adenylation entry cross-referenced to EMBL CP000117 and GenPept ABA23460.1.

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

Explore across X-Mech

AntibioticMech (mycosporine glycine) ↗ MediaIngredientMech (naturalproductmech:mibig-00a364fe41) ↗ TaxonMech: Trichormus variabilis ATCC 29413 (NCBITaxon:240292) ↗ PathwayMech (mibig:BGC0000427) ↗

Provenance

Source concept	Source	Version
BGC0000427	MIBIG	5

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