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pentalenolactone

CHEBI:70816 EXACT SEEDED antimicrobial unspecified

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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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 sesquiterpene lactone that is isolated from several Streptomyces species and exhibits antibiotic activity.

Structure

Standard InChIKeyNUPNVWUYFVEAIT-UJJBCWTCSA-N
SMILES[H][C@@]12COC(=O)[C@]3(CO3)[C@@]11C=C(C)[C@@H](C)[C@@]1([H])C=C2C(O)=O
Stereochemistryfully defined
Cross-referencespubchem:24199350, npatlas:NPA014531

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 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.

TaxonBasisClusterEvidence
Streptomyces arenae
NCBITaxon:29301		 BGC_CHARACTERIZED mibig:BGC0000653 DOI:10.1016/s0040-4039(01)88256-3
Streptomyces avermitilis MA-4680 = NBRC 14893
NCBITaxon:227882		 SOURCE_ASSERTION mibig:BGC0000678 DOI:10.1016/s0040-4039(01)88256-3

Occurrences 11

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.

TaxonSourceReference
Streptomyces
NCBITaxon:1883		 LOTUS DOI:10.1016/S0040-4039(01)95484-X
Streptomyces
NCBITaxon:1883		 LOTUS DOI:10.1021/JA00167A059
Streptomyces
NCBITaxon:1883		 LOTUS DOI:10.7164/ANTIBIOTICS.38.1114
Streptomyces avermitilis
NCBITaxon:33903		 LOTUS DOI:10.1021/BI060419N
Streptomyces avermitilis
NCBITaxon:33903		 LOTUS DOI:10.1021/BI900766W
Streptomyces avermitilis
NCBITaxon:33903		 LOTUS DOI:10.1038/JA.2010.135
Streptomyces collinus
NCBITaxon:42684		 LOTUS DOI:10.1007/S10295-015-1685-7
Streptomyces arenae
NCBITaxon:29301		 LOTUS DOI:10.1007/BF01692859
Streptomyces arenae
NCBITaxon:29301		 LOTUS DOI:10.1016/0378-1097(91)90494-U
Streptomyces arenae
NCBITaxon:29301		 LOTUS DOI:10.1128/JB.171.12.6696-6702.1989
Streptomyces arenae
NCBITaxon:29301		 LOTUS DOI:10.7164/ANTIBIOTICS.39.266

Biosynthetic gene clusters 2

AccessionHostLocus evidenceGenome
mibig:BGC0000653 Streptomyces arenae
NCBITaxon:29301 		CLUSTER_DEMONSTRATED genbank:HQ292065.1
mibig:BGC0000678 Streptomyces avermitilis MA-4680 = NBRC 14893
NCBITaxon:227882 		CLUSTER_UNSTATED genbank:BA000030.3

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.

StepEnzymeReactionSubstrate → productEvidence
1 PntA
UniProtKB:E3VWJ0		 RHEA:18081 CHEBI:175763 → CHEBI:17251 + CHEBI:33019 DOI:10.1016/j.engmic.2025.100206
2 PntI
UniProtKB:E3VWJ1		 CHEBI:17251 → CHEBI:68832 DOI:10.1016/j.engmic.2025.100206
10 Pentalenolactone D synthase
UniProtKB:E3VWI7		 RHEA:34635 CHEBI:70780 + CHEBI:57783 + CHEBI:15379 + CHEBI:15378 → CHEBI:70787 + CHEBI:58349 + CHEBI:15377 DOI:10.1021/bi1019786
20 Pentalenolactone F synthase
UniProtKB:E3VWI8		 RHEA:34579 CHEBI:70787 + CHEBI:16810 + CHEBI:15379 → CHEBI:70789 + CHEBI:30031 + CHEBI:16526 + CHEBI:15377 DOI:10.1021/bi1019786
30 Pentalenolactone synthase
UniProtKB:E3VWI3		 RHEA:34575 CHEBI:70809 → CHEBI:70816 DOI:10.1021/ja111279h

Step 1: Early cyclization step; the reaction identifier grounds chemistry, not protein identity.

Step 2: Net oxidation, not carbon-addition chemistry. The intervening hydroxylation and dehydrogenation before the existing PntE step remain unrepresented.

Step 10: Streptomyces arenae PntE catalyzes the flavin-dependent Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenate to pentalenolactone D; PntD-catalyzed formation of pentalenolactone F is represented separately.

Step 20: Streptomyces arenae PntD catalyzes 2-oxoglutarate- and Fe(2+)-dependent oxidation of pentalenolactone D to pentalenolactone F; RHEA:34579 grounds the full net reaction to the pH 7.3 pentalenolactone F conjugate base with two 2-oxoglutarate/O2 equivalents per pentalenolactone F.

Step 30: Streptomyces arenae PntM/CYP161C2 catalyzes the terminal oxidative rearrangement of pentalenolactone F to pentalenolactone; upstream PntE and PntD steps are represented separately.

Mechanism & Biosynthesis Overview

PRODUCERS & OCCURRENCE 2 producers (1 causal) 11 cited occurrences BIOSYNTHETIC LOCUS 2 gene clusters 5 curated pathway steps NATURAL PRODUCT pentalenolactone CHEBI:70816 Terpenoids TARGETS & BIOACTIVITY 0 molecular targets 0 bioactivities · 7 graphs

Causal graph — biosynthesis 3 nodes, 2 edges

Streptomyces arenae PntM-catalyzed terminal oxidative rearrangement of pentalenolactone F to pentalenolactone.

SubjectPredicateObjectNotesEvidence
pentalenolactone F is oxidatively rearranged by PntM
DOI:10.1021/ja111279h
https://mibig.secondarymetabolites.org/repository/BGC0000653.5/
https://www.uniprot.org/uniprotkb/E3VWI3
  • reference
    DOI:10.1021/ja111279h
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    PenM and PntM both catalyzed the oxidative rearrangement of 4 to 1
    notes
    The source identifies compound 4 as pentalenolactone F and compound 1 as pentalenolactone; recombinant Streptomyces arenae PntM/CYP161C2 converted pentalenolactone F to pentalenolactone in vitro.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000653.5/
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    MIBiG entry version 5 links BGC0000653 to pentalenolactone biosynthesis in Streptomyces arenae.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWI3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    UniProtKB:E3VWI3 is the reviewed Streptomyces arenae PntM/CYP161C2 gene product from HQ292065 and annotates EC:1.14.19.8/RHEA:34575 for the pentalenolactone F to pentalenolactone oxidative rearrangement.
PntM forms pentalenolactone
DOI:10.1021/ja111279h
https://mibig.secondarymetabolites.org/repository/BGC0000653.5/
https://www.uniprot.org/uniprotkb/E3VWI3
  • reference
    DOI:10.1021/ja111279h
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    PenM and PntM both catalyzed the oxidative rearrangement of 4 to 1
    notes
    The source identifies compound 4 as pentalenolactone F and compound 1 as pentalenolactone; recombinant Streptomyces arenae PntM/CYP161C2 converted pentalenolactone F to pentalenolactone in vitro.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000653.5/
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    MIBiG entry version 5 links BGC0000653 to pentalenolactone biosynthesis in Streptomyces arenae.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWI3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    UniProtKB:E3VWI3 is the reviewed Streptomyces arenae PntM/CYP161C2 gene product from HQ292065 and annotates EC:1.14.19.8/RHEA:34575 for the pentalenolactone F to pentalenolactone oxidative rearrangement.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Streptomyces arenae PntE-catalyzed Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenate to pentalenolactone D.

SubjectPredicateObjectNotesEvidence
1-deoxy-11-oxopentalenate is oxidized by PntE
DOI:10.1021/bi1019786
https://mite.lisc.univie.ac.at/repository/MITE0000057
https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
https://www.uniprot.org/uniprotkb/E3VWI7
https://www.ncbi.nlm.nih.gov/protein/ADO85575.1
https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
  • reference
    DOI:10.1021/bi1019786
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Recombinant enzymes PenE and PntE, from S. exfoliatus and S. arenae, respectively, catalyze the flavin-dependent Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenic acid (7) to pentalenolactone D (8)
    notes
    Seo et al. biochemically tested the Streptomyces arenae Tu469 PntE enzyme and placed the Baeyer-Villiger oxidation upstream of the PntD and PntM steps toward pentalenolactone.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000057
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MITE0000057 is active and links PntE to UniProtKB:E3VWI7, GenPept ADO85575.1, MIBiG BGC0000653, RHEA:34635 and the Seo et al. DOI.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MIBiG BGC0000653.5 places ADO85575.1 in the active Streptomyces arenae pentalenolactone biosynthetic gene cluster as pntE/PntE with a MITE0000057 100% identity gene-function annotation.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWI7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    UniProtKB:E3VWI7 is reviewed Streptomyces arenae PntE and annotates RHEA:34635 for 1-deoxy-11-oxopentalenate conversion to pentalenolactone D.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ADO85575.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    NCBI Protein ADO85575.1 is a 589 aa Streptomyces arenae PntE Baeyer-Villiger monooxygenase.
  • reference
    https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    The Rhea-to-UniProtKB Swiss-Prot mapping links RHEA:34635 to UniProtKB:E3VWI7.
PntE forms pentalenolactone D
DOI:10.1021/bi1019786
https://mite.lisc.univie.ac.at/repository/MITE0000057
https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
https://www.uniprot.org/uniprotkb/E3VWI7
https://www.ncbi.nlm.nih.gov/protein/ADO85575.1
https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
  • reference
    DOI:10.1021/bi1019786
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Recombinant enzymes PenE and PntE, from S. exfoliatus and S. arenae, respectively, catalyze the flavin-dependent Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenic acid (7) to pentalenolactone D (8)
    notes
    Seo et al. biochemically tested the Streptomyces arenae Tu469 PntE enzyme and placed the Baeyer-Villiger oxidation upstream of the PntD and PntM steps toward pentalenolactone.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000057
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MITE0000057 is active and links PntE to UniProtKB:E3VWI7, GenPept ADO85575.1, MIBiG BGC0000653, RHEA:34635 and the Seo et al. DOI.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MIBiG BGC0000653.5 places ADO85575.1 in the active Streptomyces arenae pentalenolactone biosynthetic gene cluster as pntE/PntE with a MITE0000057 100% identity gene-function annotation.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWI7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    UniProtKB:E3VWI7 is reviewed Streptomyces arenae PntE and annotates RHEA:34635 for 1-deoxy-11-oxopentalenate conversion to pentalenolactone D.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ADO85575.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    NCBI Protein ADO85575.1 is a 589 aa Streptomyces arenae PntE Baeyer-Villiger monooxygenase.
  • reference
    https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    The Rhea-to-UniProtKB Swiss-Prot mapping links RHEA:34635 to UniProtKB:E3VWI7.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Streptomyces arenae PntD-catalyzed oxidation of pentalenolactone D to pentalenolactone F.

SubjectPredicateObjectNotesEvidence
pentalenolactone D is oxidized by PntD
DOI:10.1021/bi1019786
https://mite.lisc.univie.ac.at/repository/MITE0000058
https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
https://www.uniprot.org/uniprotkb/E3VWI8
https://www.ncbi.nlm.nih.gov/protein/ADO85576.1
https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
  • reference
    DOI:10.1021/bi1019786
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    pentalenolactone D (8) to pentalenolactone E (15) and pentalenolactone F (16)
    notes
    Seo et al. biochemically tested recombinant Streptomyces arenae Tu469 PntD and reported 2-oxoglutarate- and Fe(2+)-dependent oxidation of pentalenolactone D to pentalenolactones E and F; native pntD mutants accumulated pentalenolactone D and lost pentalenolactone, pentalenolactone E and pentalenolactone F.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000058
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MITE0000058 is active and links PntD to UniProtKB:E3VWI8, GenPept ADO85576.1, MIBiG BGC0000653, RHEA:34579, EC:1.14.11.36 and the Seo et al. DOI.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MIBiG BGC0000653.5 places ADO85576.1 in the active Streptomyces arenae pentalenolactone biosynthetic gene cluster as pntD/PntD with a MITE0000058 100% identity gene-function annotation.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWI8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    UniProtKB:E3VWI8 is reviewed Streptomyces arenae PntD, cross-links GenPept ADO85576.1, and annotates RHEA:34579 for the net 2-oxoglutarate- and O2-dependent conversion of pentalenolactone D to pentalenolactone F.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ADO85576.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    NCBI Protein ADO85576.1 is a 299 aa Streptomyces arenae PntD.
  • reference
    https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    The Rhea-to-UniProtKB Swiss-Prot mapping links RHEA:34579 to UniProtKB:E3VWI8.
PntD forms pentalenolactone F(1-)
DOI:10.1021/bi1019786
https://mite.lisc.univie.ac.at/repository/MITE0000058
https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
https://www.uniprot.org/uniprotkb/E3VWI8
https://www.ncbi.nlm.nih.gov/protein/ADO85576.1
https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
  • reference
    DOI:10.1021/bi1019786
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    pentalenolactone D (8) to pentalenolactone E (15) and pentalenolactone F (16)
    notes
    Seo et al. biochemically tested recombinant Streptomyces arenae Tu469 PntD and reported 2-oxoglutarate- and Fe(2+)-dependent oxidation of pentalenolactone D to pentalenolactones E and F; native pntD mutants accumulated pentalenolactone D and lost pentalenolactone, pentalenolactone E and pentalenolactone F.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000058
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MITE0000058 is active and links PntD to UniProtKB:E3VWI8, GenPept ADO85576.1, MIBiG BGC0000653, RHEA:34579, EC:1.14.11.36 and the Seo et al. DOI.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000653.5/BGC0000653.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    MIBiG BGC0000653.5 places ADO85576.1 in the active Streptomyces arenae pentalenolactone biosynthetic gene cluster as pntD/PntD with a MITE0000058 100% identity gene-function annotation.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWI8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    UniProtKB:E3VWI8 is reviewed Streptomyces arenae PntD, cross-links GenPept ADO85576.1, and annotates RHEA:34579 for the net 2-oxoglutarate- and O2-dependent conversion of pentalenolactone D to pentalenolactone F.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ADO85576.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    NCBI Protein ADO85576.1 is a 299 aa Streptomyces arenae PntD.
  • reference
    https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-01
    notes
    The Rhea-to-UniProtKB Swiss-Prot mapping links RHEA:34579 to UniProtKB:E3VWI8.

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

Causal graph — biosynthesis 5 nodes, 4 edges

S. arenae TU469 early biosynthesis, supported by heterologous expression. The acid endpoint is upstream of the separately curated late reactions, not pentalenolactone itself.

SubjectPredicateObjectNotesEvidence
2-trans,6-trans-farnesyl diphosphate(3-) is cyclized by PntA
DOI:10.1016/j.engmic.2025.100206
https://www.uniprot.org/uniprotkb/E3VWJ0
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 3, pntA-only control.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWJ0
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    S. arenae Tu469 PntA, 337 aa; exact sequence match to ADO85578.1 from HQ292065.1:13164..14177. UniProt assigns RHEA:18081; protein grounding denotes the native gene product, not an affinity-tagged construct.
PntA forms pentalenene
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    GC-MS identification in the pntA-only expression strain.
pentalenene is oxidized by PntI
DOI:10.1016/j.engmic.2025.100206
https://www.uniprot.org/uniprotkb/E3VWJ1
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Net allylic oxidation in heterologous hosts.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWJ1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    S. arenae TU469 PntI, 457 aa; exact sequence match to ADO85579.1 from HQ292065.1:14292..15665. This unreviewed entry supplies sequence identity, not the experimental activity assignment from the newer paper.
PntI forms 1-deoxypentalenic acid
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Product 6; methylation is analytical derivatization.

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

Causal graph — biosynthesis 6 nodes, 5 edges

UC5319 PenA cyclization and the native penI deletion phenotype. Purified PenA evidence and genetic PenI evidence are distinct; the deletion does not establish an isolated PenI reaction or exclude indirect effects.

SubjectPredicateObjectNotesEvidence
2-trans,6-trans-farnesyl diphosphate(3-) is cyclized by PenA
DOI:10.1021/bi00185a024
https://www.uniprot.org/uniprotkb/Q55012
  • reference
    DOI:10.1021/bi00185a024
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Abstract: purified native and recombinant UC5319 synthase; both require Mg2+.
    snippet
    catalyzes the cyclization of farnesyl diphosphate
  • reference
    https://www.uniprot.org/uniprotkb/Q55012
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    UC5319 PenA, 337 aa; exact sequence match to both original clone AAA19131.1/U05213.1 and ADO85594.1/HQ292066.1. The 1994 source names Streptomyces UC5319; the cluster and 2025 paper name S. exfoliatus.
PenA forms pentalenene
DOI:10.1021/bi00185a024
  • reference
    DOI:10.1021/bi00185a024
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Purified UC5319 pentalenene synthase converts FPP to pentalenene.
PenI encoding gene is disrupted in In-frame penI deletion in S. exfoliatus UC5319
DOI:10.1016/j.engmic.2025.100206
https://www.uniprot.org/uniprotkb/E3VWK7
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Main-text deletion paragraph and Figure S1: CD2 replaces an internal 1194-bp penI fragment with an NdeI site. Table S1's pntI label for CD2 conflicts with the main text and pWHU1708 construct in Table S2; the latter identify penI.
    snippet
    an internal 1194-bp fragment
  • reference
    https://www.uniprot.org/uniprotkb/E3VWK7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    UC5319 PenI, 463 aa; exact match to ADO85595.1 at HQ292066.1:11705..13096. Identifier denotes the native protein, not the in-frame deletion construct. Sequence grounding alone does not establish a specific oxidation reaction.
In-frame penI deletion in S. exfoliatus UC5319 abolishes detectable production of pentalenolactone
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 2A-C: wild-type UC5319 produces 1, but CD2 lacks detectable 1. Acidified extracts were methylated before GC-MS; 1-Me is the analytical derivative, not the biosynthetic product.
In-frame penI deletion in S. exfoliatus UC5319 causes accumulation of pentalenene
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 2C-D identifies accumulated compound 3 in CD2. This genetic observation does not by itself prove PenI catalyzes all three oxidation steps to the acid.

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

Causal graph — biosynthesis 14 nodes, 14 edges

PtlI from the S. avermitilis neopentalenolactone pathway acts on shared early precursors. The 2006 purified assay and 2025 engineered PenA/PtlI E. coli experiment are separate contexts. Neither establishes native S. avermitilis production of pentalenolactone. E. coli FldA/Fdr reconstitution is distinct from the FdxD/FprD test that reported no detectable acid; the latter is not a native-partner assignment.

SubjectPredicateObjectNotesEvidence
PtlI catalyzes Purified PtlI oxidation with E. coli Fld/Fdr
DOI:10.1021/ja0639214
https://www.uniprot.org/uniprotkb/Q82IY3
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Recombinant His6-tagged PtlI was assayed with E. coli flavodoxin/flavodoxin reductase and NADPH, not native redox partners.
  • reference
    https://www.uniprot.org/uniprotkb/Q82IY3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    PtlI/SAV_2999, 449 aa, exact match to BAC70710.1. NRRL 8165 and MA-4680 are aliases of the same S. avermitilis strain. Canonical accession excludes the 2006 C-terminal His6 tag. UniProt annotates the native pathway as neopentalenolactone, not pentalenolactone production in vivo.
Racemic pentalenene assay substrate is substrate for Purified PtlI oxidation with E. coli Fld/Fdr
DOI:10.1021/ja0639214
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    The 2006 substrate was synthetic racemic pentalenene; the mixture is not assigned the enantiopure CHEBI:17251 identifier.
Purified PtlI oxidation with E. coli Fld/Fdr forms pentalen-13-ol
DOI:10.1021/ja0639214
https://pubchem.ncbi.nlm.nih.gov/compound/56927746
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Chiral GC-MS identified a single alcohol enantiomer from racemic pentalenene; the separate alcohol-feeding assay also had background oxidation.
    snippet
    by stepwise allylic oxidation via pentalen-13-ol
  • reference
    https://pubchem.ncbi.nlm.nih.gov/compound/56927746
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    ChEBI-sourced structure cross-reference CHEBI:63243; natural pentalen-13-ol, UUWZJPBRBCIXLA-IKVITTDRSA-N.
Purified PtlI oxidation with E. coli Fld/Fdr forms pentalen-13-al
DOI:10.1021/ja0639214
https://www.rhea-db.org/rhea/31699
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Chiral GC-MS identified a single aldehyde enantiomer. The original report detected only trace acid under varied conditions and left efficient aldehyde-to-acid conversion unresolved.
  • reference
    https://www.rhea-db.org/rhea/31699
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    Rhea grounds the natural pentalen-13-al product to CHEBI:63244, JWMGZDVPJPOYGL-IKVITTDRSA-N; the reaction ID is not a protein ID.
PenA forms pentalenene
DOI:10.1016/j.engmic.2025.100206
https://www.uniprot.org/uniprotkb/Q55012
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 4A penA-only control produces pentalenene; Table S2 traces pLJ5 to UC5319 penA in pLJ1.
  • reference
    https://www.uniprot.org/uniprotkb/Q55012
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    UC5319 PenA, 337 aa; exact sequence match to both original clone AAA19131.1/U05213.1 and ADO85594.1/HQ292066.1. The 1994 source names Streptomyces UC5319; the cluster and 2025 paper name S. exfoliatus.
pentalenene is substrate for PenA/PtlI oxidation in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 4B and Table S2: pLJ80 adds NRRL 8165 ptlI from pWHU1607 to the PenA host BL21(DE3) carrying pMH1/pFZ81.
PtlI supports PenA/PtlI oxidation in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
https://www.uniprot.org/uniprotkb/Q82IY3
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 4B is a whole-cell experiment, not a purified three-step reconstitution. Host redox metabolism may contribute.
  • reference
    https://www.uniprot.org/uniprotkb/Q82IY3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    PtlI/SAV_2999, 449 aa, exact match to BAC70710.1. NRRL 8165 and MA-4680 are aliases of the same S. avermitilis strain. Canonical accession excludes the 2006 C-terminal His6 tag. UniProt annotates the native pathway as neopentalenolactone, not pentalenolactone production in vivo.
PenA/PtlI oxidation in engineered E. coli forms 1-deoxypentalenic acid
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Compound 6 was detected as 6-Me after acidification and methylation. This is an intermediate endpoint, not production of final pentalenolactone.
    snippet
    6 was detected (Fig. 4B and C)
E. coli FldA is supplied in Purified PtlI oxidation with E. coli Fld/Fdr
DOI:10.1021/ja0639214
https://www.uniprot.org/uniprotkb/P61949
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Reference 15a identifies the assay flavodoxin by accession; this supplied redox protein is not a native S. avermitilis partner.
    snippet
    FldA, Swissprot P61949
  • reference
    https://www.uniprot.org/uniprotkb/P61949
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    E. coli K12 fldA, 176 aa; exact match to NP_415210.1/b0684. The accession is explicitly named in the PtlI paper, not inferred from the BL21(DE3) expression host.
E. coli Fdr is supplied in Purified PtlI oxidation with E. coli Fld/Fdr
DOI:10.1021/ja0639214
https://www.uniprot.org/uniprotkb/P28861
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Reference 15b identifies Fdr. Supplied with FldA and NADPH in the purified PtlI assay, not a demonstrated physical complex.
    snippet
    Fdr, Swissprot P28861
  • reference
    https://www.uniprot.org/uniprotkb/P28861
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    E. coli K12 fpr, 248 aa; exact match to NP_418359.1/b3924. Fdr is the paper's label for NADPH-flavodoxin reductase; it is distinct from S. avermitilis FprD.
S. avermitilis FdxD is supplied in In-vitro PtlI test with FdxD/FprD
DOI:10.1021/ja0639214
https://www.uniprot.org/uniprotkb/Q82IK4
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Note 17 names SAV3129 in this separate redox-pair test.
  • reference
    https://www.uniprot.org/uniprotkb/Q82IK4
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    MA-4680 FdxD, 106 aa; exact match to BAC70840.1, SAVERM_3129 (old SAV_3129), complement(BA000030.4:3901642..3901962). Identity grounding is not a productive-partner assignment.
S. avermitilis FprD is supplied in In-vitro PtlI test with FdxD/FprD
DOI:10.1021/ja0639214
https://www.uniprot.org/uniprotkb/Q82BM9
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Note 17 names SAV5675 with FdxD, not the E. coli Fdr protein.
  • reference
    https://www.uniprot.org/uniprotkb/Q82BM9
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    MA-4680 FprD, 421 aa; exact match to BAC73387.1, SAVERM_5675 (old SAV_5675), BA000030.4:6862850..6864115. The unreviewed annotation supplies sequence identity.
PtlI is assayed in In-vitro PtlI test with FdxD/FprD
DOI:10.1021/ja0639214
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Note 17 reports no enhancement of pentalenene oxidation; the comparison and quantitative detection limit are not specified.
In-vitro PtlI test with FdxD/FprD has no reported detectable formation of 1-deoxypentalenic acid
DOI:10.1021/ja0639214
  • reference
    DOI:10.1021/ja0639214
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Note 17's condition-specific result does not erase trace acid reported elsewhere or prove incapacity under other conditions.
    snippet
    no detectable formation

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

Causal graph — biosynthesis 15 nodes, 19 edges

Engineered E. coli BL21(DE3) with PenA/PntI and alternative J1074 redox-gene expression conditions. XNR_5179-containing pairs increased intermediate production; XNR_1673 conditions are represented only as tested conditions. Neither native partnership, physical complex, nor increased final pentalenolactone yield is asserted.

SubjectPredicateObjectNotesEvidence
PntI supports 1-deoxypentalenic acid production in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
https://www.uniprot.org/uniprotkb/E3VWJ1
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 4C, PenA/PntI host.
  • reference
    https://www.uniprot.org/uniprotkb/E3VWJ1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    S. arenae TU469 PntI, 457 aa; exact sequence match to ADO85579.1 from HQ292065.1:14292..15665. This unreviewed entry supplies sequence identity, not the experimental activity assignment from the newer paper.
XNR_5179 ferredoxin is coexpressed in Joint expression of XNR_5179 and XNR_4478
DOI:10.1016/j.engmic.2025.100206
https://www.ncbi.nlm.nih.gov/protein/AGI91495.1
https://rest.uniprot.org/uniparc/UPI0001CE8D5E.json
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table S2: J1074 gene in pLJ62.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI91495.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    XNR_5179 encodes a 100-aa ferredoxin at complement(CP004370.1:5881185..5881487), strain J1074. NCBI names this strain S. albidoflavus (taxon 1886); the paper uses S. albus. Exact-locus and GenPept-cross-reference UniProt queries did not resolve an accession; no homolog was substituted.
  • reference
    https://rest.uniprot.org/uniparc/UPI0001CE8D5E.json
    evidence type
    DATABASE_ASSERTION
    notes
    UniParc UPI0001CE8D5E (100 aa) links active EMBL AGI91495.1 (Streptomyces albus J1074, taxon 457425, locus XNR_5179) and inactive UniProtKB/TrEMBL D6BAD9 (ScoT_55270), K1UZQ9 (SM8_03262) and A0A0S1UWG1 (SFR_6044), with zero active UniProtKB cross-references.
    retrieved on
    2026-10-30
XNR_4478 ferredoxin reductase is coexpressed in Joint expression of XNR_5179 and XNR_4478
DOI:10.1016/j.engmic.2025.100206
https://www.ncbi.nlm.nih.gov/protein/AGI90801.1
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table S2: J1074 gene in pLJ62.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI90801.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    XNR_4478 encodes a 420-aa ferredoxin reductase at complement(CP004370.1:5093104..5094366), strain J1074, currently S. albidoflavus in NCBI and S. albus in the paper. Retained the versioned NCBI Protein accession after exact-locus and GenPept-cross-reference UniProt queries returned no match.
Joint expression of XNR_5179 and XNR_4478 increases 1-deoxypentalenic acid production in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 5: the pair improved yield relative to PenA/PntI alone; the authors reported no significant change for individual additions.
PenA supplies pentalenene for 1-deoxypentalenic acid production in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
https://www.uniprot.org/uniprotkb/Q55012
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figures 4A and 5: the E. coli strains carry UC5319 penA; PenA is not the TU469 PntA used in the Streptomyces experiment.
  • reference
    https://www.uniprot.org/uniprotkb/Q55012
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    UC5319 PenA, 337 aa; exact sequence match to both original clone AAA19131.1/U05213.1 and ADO85594.1/HQ292066.1. The 1994 source names Streptomyces UC5319; the cluster and 2025 paper name S. exfoliatus.
XNR_4772 predicted ferredoxin reductase is coexpressed in Joint expression of XNR_5179 and XNR_4772
DOI:10.1016/j.engmic.2025.100206
https://www.ncbi.nlm.nih.gov/protein/AGI91094.1
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table S2: pLJ52 carries J1074 XNR_4772, transferred via pLJ55 to pLJ64. Figure 5 and Tables S2-S4 use XNR_4772; an earlier main-text occurrence of XNR_4722 is inconsistent.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI91094.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    395-aa XNR_4772 at CP004370.1:5424795..5425982, strain J1074. NCBI calls this S. albidoflavus; the paper calls it S. albus. Exact-locus and GenPept-cross-reference UniProt searches did not resolve an accession; no homolog was substituted. NCBI labels it oxidoreductase; the paper selects it as a predicted FDR.
XNR_5179 ferredoxin is coexpressed in Joint expression of XNR_5179 and XNR_4772
DOI:10.1016/j.engmic.2025.100206
https://www.ncbi.nlm.nih.gov/protein/AGI91495.1
https://rest.uniprot.org/uniparc/UPI0001CE8D5E.json
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table S2: XNR_5179 from pLJ54 is added to pLJ55 to make pLJ64, jointly expressing the two J1074 redox proteins.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI91495.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    XNR_5179 encodes a 100-aa ferredoxin at complement(CP004370.1:5881185..5881487), strain J1074. NCBI names this strain S. albidoflavus (taxon 1886); the paper uses S. albus. Exact-locus and GenPept-cross-reference UniProt queries did not resolve an accession; no homolog was substituted.
  • reference
    https://rest.uniprot.org/uniparc/UPI0001CE8D5E.json
    evidence type
    DATABASE_ASSERTION
    notes
    UniParc UPI0001CE8D5E (100 aa) links active EMBL AGI91495.1 (Streptomyces albus J1074, taxon 457425, locus XNR_5179) and inactive UniProtKB/TrEMBL D6BAD9 (ScoT_55270), K1UZQ9 (SM8_03262) and A0A0S1UWG1 (SFR_6044), with zero active UniProtKB cross-references.
    retrieved on
    2026-10-30
Joint expression of XNR_5179 and XNR_4772 increases 1-deoxypentalenic acid production in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 5 compares pLJ64 with PenA/PntI-only pLJ9. The paired condition increased acid production; the authors reported no significant change for individual additions. No physical complex or native partnership is demonstrated.
XNR_1673 ferredoxin is expressed in XNR_1673 addition to PenA/PntI
DOI:10.1016/j.engmic.2025.100206
https://www.ncbi.nlm.nih.gov/protein/AGI88059.1
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table S2 traces J1074 XNR_1673 from pLJ53 to pLJ56; the host contains pMH1, pFZ81 and PenA/PntI.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI88059.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-03
    notes
    J1074 XNR_1673, 106 aa, complement(CP004370.1:1979389..1979709). NCBI uses S. albidoflavus; the paper uses S. albus. UniProt query (AGI88059 OR gene:XNR_1673) returned no results; the versioned NCBI accession avoids substituting a homolog.
XNR_1673 addition to PenA/PntI was tested for effects on 1-deoxypentalenic acid production in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Figure 5, pLJ56 versus pLJ9: the authors reported no significant change for individual additions. This is not evidence of zero effect or intrinsic inactivity.
    snippet
    no significant change in the yield of 6
XNR_1673 ferredoxin is coexpressed in Joint expression of XNR_1673 and XNR_4478
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table S2: pLJ61 adds XNR_1673 from pLJ53 to pLJ10.
XNR_4478 ferredoxin reductase is coexpressed in Joint expression of XNR_1673 and XNR_4478
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    pLJ10 supplies XNR_4478 to the pLJ61 paired condition.
XNR_1673 ferredoxin is coexpressed in Joint expression of XNR_1673 and XNR_4772
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table S2: pLJ63 adds XNR_1673 from pLJ53 to pLJ55.
XNR_4772 predicted ferredoxin reductase is coexpressed in Joint expression of XNR_1673 and XNR_4772
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    pLJ55 supplies XNR_4772 to the pLJ63 paired condition.
Joint expression of XNR_1673 and XNR_4478 was tested for effects on 1-deoxypentalenic acid production in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    pLJ61 versus pLJ9: main text reports unchanged yield, but Figure 5 plots a higher mean. No causal null or statistical significance is inferred from this discrepancy.
    snippet
    the yield of 6 did not change
Joint expression of XNR_1673 and XNR_4772 was tested for effects on 1-deoxypentalenic acid production in engineered E. coli
DOI:10.1016/j.engmic.2025.100206
  • reference
    DOI:10.1016/j.engmic.2025.100206
    evidence type
    PRIMARY_EXPERIMENT
    notes
    pLJ63 versus pLJ9: main text reports unchanged yield, but Figure 5 plots a higher mean. This edge records testing, not a demonstrated absence of an effect.
XNR_4478 ferredoxin reductase has a sequence-identical UniProtKB example XNR_4478 ferredoxin reductase (S. albidoflavus FRZ02_28405 UniProtKB example) UniProtKB:D6AZ77 (Streptomyces albidoflavus FRZ02_28405) shares 100% amino-acid sequence identity (UPI0001AEE243) with Streptomyces albus J1074 XNR_4478 (AGI90801.1).
https://www.uniprot.org/uniprotkb/D6AZ77
https://www.uniprot.org/uniparc/UPI0001AEE243
https://www.ncbi.nlm.nih.gov/protein/AGI90801.1
  • reference
    https://www.uniprot.org/uniprotkb/D6AZ77
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    Active Streptomyces albidoflavus UniProtKB entry (D6AZ77, FRZ02_28405) for the UPI0001AEE243 ferredoxin-NADP reductase sequence.
  • reference
    https://www.uniprot.org/uniparc/UPI0001AEE243
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    UniParc UPI0001AEE243 links CP004370.1 AGI90801.1 (XNR_4478) and active Streptomyces albidoflavus UniProtKB:D6AZ77 under a single 100%-identical sequence.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI90801.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    CP004370.1 GenPept AGI90801.1 is the Streptomyces albus J1074 XNR_4478 ferredoxin reductase translation.
XNR_1673 ferredoxin has a sequence-identical UniProtKB example XNR_1673 ferredoxin (S. albidoflavus FRZ02_12020 UniProtKB example) UniProtKB:D6B5H4 (Streptomyces albidoflavus FRZ02_12020) shares 100% amino-acid sequence identity (UPI0001AEEB06) with Streptomyces albus J1074 XNR_1673 (AGI88059.1).
https://www.uniprot.org/uniprotkb/D6B5H4
https://www.uniprot.org/uniparc/UPI0001AEEB06
https://www.ncbi.nlm.nih.gov/protein/AGI88059.1
  • reference
    https://www.uniprot.org/uniprotkb/D6B5H4
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    Active Streptomyces albidoflavus UniProtKB entry (D6B5H4, FRZ02_12020) for the UPI0001AEEB06 ferredoxin sequence.
  • reference
    https://www.uniprot.org/uniparc/UPI0001AEEB06
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    UniParc UPI0001AEEB06 links CP004370.1 AGI88059.1 (XNR_1673) and active Streptomyces albidoflavus UniProtKB:D6B5H4 under a single 100%-identical sequence.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI88059.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    CP004370.1 GenPept AGI88059.1 is the Streptomyces albus J1074 XNR_1673 ferredoxin translation.
XNR_4772 predicted ferredoxin reductase has a sequence-identical UniProtKB example XNR_4772 predicted ferredoxin reductase (S. wadayamensis DC60_00205 UniProtKB example) UniProtKB:A0ABR4S4L1 (Streptomyces wadayamensis DC60_00205, S. albidoflavus clade) shares 100% amino-acid sequence identity (UPI0001AECE6D) with Streptomyces albus J1074 XNR_4772 (AGI91094.1).
https://www.uniprot.org/uniprotkb/A0ABR4S4L1
https://www.uniprot.org/uniparc/UPI0001AECE6D
https://www.ncbi.nlm.nih.gov/protein/AGI91094.1
  • reference
    https://www.uniprot.org/uniprotkb/A0ABR4S4L1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    Active Streptomyces wadayamensis UniProtKB entry (A0ABR4S4L1, DC60_00205) for the UPI0001AECE6D pyridine nucleotide-disulfide oxidoreductase sequence.
  • reference
    https://www.uniprot.org/uniparc/UPI0001AECE6D
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    UniParc UPI0001AECE6D links CP004370.1 AGI91094.1 (XNR_4772) and active UniProtKB:A0ABR4S4L1 under a single 100%-identical sequence.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AGI91094.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-17
    notes
    CP004370.1 GenPept AGI91094.1 is the Streptomyces albus J1074 XNR_4772 translation.

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

Elsewhere in the fleet

Explore across X-Mech

AntibioticMech (pentalenolactone) ↗ MediaIngredientMech (CHEBI:70816) ↗ TaxonMech: Streptomyces arenae (NCBITaxon:29301) ↗ TaxonMech: Streptomyces avermitilis MA-4680 = NBRC 14893 (NCBITaxon:227882) ↗ PathwayMech (mibig:BGC0000653) ↗ PathwayMech (mibig:BGC0000678) ↗

Open questions 1

shared-structure — This structure is reported by more than one MIBiG entry: BGC0000653, BGC0000678. Confirm they describe the same compound rather than an upstream cross-reference error.

Provenance

Source conceptSourceVersion
BGC0000653MIBIG5
BGC0000678MIBIG5
CHEBI:70816CHEBI3-star

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