everninomicin D
naturalproductmech:mibig-22fed17184 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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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 | HZLMUDOBOCVXQT-YOQBUGDQSA-N |
|---|---|
| SMILES | COC[C@H]1O[C@@H](O[C@@H]2OC[C@@H]3O[C@@]4(OC[C@@](O)([C@H](C)OC)[C@@H]5OCO[C@H]54)O[C@H]3[C@H]2OC)[C@@H](OC)[C@@H](O)[C@@H]1O[C@@H]1O[C@H](C)[C@H](OC)[C@H](O[C@H]2C[C@@]3(C)O[C@@]4(C[C@@H](O)[C@H](O[C@H]5C[C@@H](O[C@H]6C[C@](C)([N+](=O)[O-])[C@@H](OC)[C@H](C)O6)[C@H](OC(=O)C6=C(C)C(Cl)=C(O)C(Cl)=C6OC)[C@@H](C)O5)[C@@H](C)O4)O[C@@H]3[C@@H](C)O2)[C@H]1O |
| Stereochemistry | fully defined |
| Cross-references | pubchem:5490208, npatlas:NPA032756 |
Filing pathway
Carbohydrates — 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 saccharide, 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 |
|---|---|---|---|
| Micromonospora carbonacea NCBITaxon:47853 |
BGC_CHARACTERIZED | mibig:BGC0002085 | PMID:20866105 |
Occurrences 1
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 carbonacea NCBITaxon:47853 |
LOTUS | DOI:10.1021/JA00840A078 |
Biosynthetic gene clusters 1
| Accession | Host | Locus evidence | Genome |
|---|---|---|---|
| mibig:BGC0002085 | Micromonospora carbonacea NCBITaxon:47853 |
CLUSTER_DEMONSTRATED | genbank:CP058322.1 |
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 5 nodes, 4 edges
Partial precursor chemistry for everninomicin D: purified, N-terminal His6-tagged EvdS6 expressed from pET28a(+) in E. coli Tuner(DE3) was assayed with UDP-GlcA. UDP-4-keto-D-xylose and UDP-D-xylose are candidate precursors of the H- and G-rings, respectively. Their downstream incorporation, the native UDP-versus-TDP donor preference, and complete everninomicin D biosynthesis were not demonstrated.
| Subject | Predicate | Object | Notes | Evidence |
|---|---|---|---|---|
| UDP-D-glucuronic acid (assayed substrate) | is_assayed_substrate_of | EvdS6 N-terminal His6 construct | The identifier denotes the native 329-aa parent QLD23489.2, not the affinity tag. It is HXZ27_04045 at CP058322.1:898338..899327, called evdS5 in GenBank and MIBiG BGC0002085.3 but EvdS6 in this paper. The CDS translation and GenPept sequence match both PDB constructs after accounting for the 19-aa MGSSHHHHHHSSGLVPRGS tag and the initiating GTG codon: native initiator M is V when internal to the fusion. Table S1 cloning-primer termini match this CDS. Do not substitute the adjacent evdS6-labelled HXZ27_04050/QLD23490.1. The PDB-linked UniProt A0A1C5ADV9 was rejected as an exact parent: it is 324 aa and has two internal sequence conflicts with the assayed protein, in addition to the N-terminal difference. UniParc UPI0015DCE6B0 archives the exact 329-aa QLD23489.2 sequence with zero active or inactive UniProtKB cross-references. Current GenPept assigns M. carbonacea subsp. aurantiaca, NRRL 2997, NCBITaxon:3454472; its parent is NCBITaxon:47853, the species in the pinned MIBiG record. | DOI:10.1016/j.jbc.2023.104893 |
| EvdS6 N-terminal His6 construct | produces_in_vitro | UDP-4-keto-D-xylose | HPLC-MS, 2-bromophenylhydrazine derivatization and reaction-mixture NMR establish the keto product and its D-xylose configuration; the keto group is predominantly hydrated in aqueous solution. Products were absent in the boiled-enzyme control. Standard turnover assays used 1 mM UDP-GlcA, 1 mM NAD+, 0.5 mg/ml enzyme, 50 mM HEPES pH 8.5 at 30 C for 1 h. NMR used an extended incubation and the filtered reaction mixture because purified products were unstable; no isolated-product yield is asserted. | DOI:10.1016/j.jbc.2023.104893
|
| EvdS6 N-terminal His6 construct | produces_in_vitro | UDP-D-xylose | HPLC-MS and multidimensional NMR identify the reduced D-xylose product. The Figure 3 time course used 1 mM UDP-GlcA, 0.1 mM NAD+, 0.42 mg/ml enzyme and 50 mM HEPES pH 8.5, distinct from the standard assay. Both products are seen early, whereas UDP-D-xylose predominates after overnight incubation. This is not direct production of L-lyxose or of the final antibiotic. | DOI:10.1016/j.jbc.2023.104893
|
| NAD+ | supports_assayed_turnover_of | EvdS6 N-terminal His6 construct | Figure S4A compares added NAD+, NADP+ and no exogenous cofactor at 1 mM UDP-GlcA, 0.35 mg/ml enzyme and 50 mM HEPES pH 8.5. NAD+ gives substantially greater turnover; the other conditions retain low activity. Copurified NAD+ precludes interpreting the no-added-cofactor condition as a cofactor-free enzyme. | DOI:10.1016/j.jbc.2023.104893
|
Every edge carries its own citation; an uncited edge is refused by the corpus tests.
Causal graph — biosynthesis 4 nodes, 3 edges
Structural assembly of the recombinant EvdS6 precursor enzyme, not a demonstrated in-vivo complex. PDB 8SHH (1.93 A) contains copurified NAD+ without added substrate ligand; PDB 8SK0 (1.51 A) contains NAD+ and TDP after crystallization with commercial UDP-GlcA. A PDB deposition is structural evidence, not a protein accession.
| Subject | Predicate | Object | Notes | Evidence |
|---|---|---|---|---|
| EvdS6 N-terminal His6 construct | forms_observed_homodimer | Observed recombinant EvdS6 homodimer | Two copies of the sequence-verified parent form the crystallized dimer. Both deposits have the same tagged 348-aa sequence described in the assay graph. RCSB assembly 1 is an author/PISA homodimer with gel-filtration support; no native-cell assembly measurement or distinct complex accession is asserted. | DOI:10.1016/j.jbc.2023.104893 |
| Observed recombinant EvdS6 homodimer | contains_bound_cofactor | Copurified NAD+ | NAD+ is noncovalently bound in each protomer in both structures. Thus the paper's ligand-free state must not be interpreted as wholly apo or NAD-free. | DOI:10.1016/j.jbc.2023.104893
|
| Observed recombinant EvdS6 homodimer | contains_observed_bound_ligand | Bound TDP (thymidine diphosphate) | In 8SK0, TDP is resolved in one protomer with no attached glucuronic acid. The other active site has partial citrate occupancy and unresolved mixed density. The source of TDP is uncertain; a minor substrate-stock contaminant was suggested but not detected by HPLC-MS. This structure does not establish TDP-sugar catalysis, nucleotide preference, or an unambiguous bound UDP-GlcA catalytic intermediate. | DOI:10.1016/j.jbc.2023.104893 |
Every edge carries its own citation; an uncited edge is refused by the corpus tests.
Causal graph — biosynthesis 9 nodes, 18 edges
Figure 7A reports six EvdS6 alanine variants relative to wild type, at 30 min with 1 mM UDP-GlcA, 1 mM NAD+ and 50 mM HEPES pH 8.5. Relative turnover is based on HPLC-MS extracted-ion peak areas, not kinetic constants; six measurements comprise three biological replicates with two technical replicates each. Residue numbering matches native parent QLD23489.2. No mutant-specific accession is assigned here; these constructs are not equated to the native sequence. The R278A and R279A construct identities need review because of a Table S1 primer-label discrepancy; their edges preserve reported results. UniParc UPI0015DCE6B0 (329 aa) links active EMBL QLD23489.2 with zero active or inactive UniProtKB entries.
| Subject | Predicate | Object | Notes | Evidence |
|---|---|---|---|---|
| Reported EvdS6 H87A construct | reported_decreased | UDP-4-keto-D-xylose formation at 30 min | The paper reports decreased formation of both products, with no reported alteration of their ratio. This does not establish a direct chemical role for H87; structural explanations remain hypotheses. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 H87A construct | reported_decreased | UDP-D-xylose formation at 30 min | The paper reports decreased formation of both products, with no reported alteration of their ratio. This does not establish a direct chemical role for H87; structural explanations remain hypotheses. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 T126A construct | reported_no_significant_change_in | UDP-4-keto-D-xylose formation at 30 min | The reduced product is minimally detectable while the keto-product readout is not significantly different from wild type. This supports a role in reduction without proving a specific hydride-transfer mechanism. The Table S1 primer pair matches T126A when its orientation is accounted for. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 T126A construct | reported_minimal | UDP-D-xylose formation at 30 min | The reduced product is minimally detectable while the keto-product readout is not significantly different from wild type. This supports a role in reduction without proving a specific hydride-transfer mechanism. The Table S1 primer pair matches T126A when its orientation is accounted for. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 E128A construct | reported_no_significant_change_in | UDP-4-keto-D-xylose formation at 30 min | Neither product readout differs significantly from wild type in this assay. This is not proof that E128 lacks a catalytic contribution, nor evidence for the proposed compensatory role of D127. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 E128A construct | reported_no_significant_change_in | UDP-D-xylose formation at 30 min | Neither product readout differs significantly from wild type in this assay. This is not proof that E128 lacks a catalytic contribution, nor evidence for the proposed compensatory role of D127. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 N179A construct | reported_decreased | UDP-4-keto-D-xylose formation at 30 min | Keto-product formation decreases and reduced-product formation is minimal. N179 is asparagine, as shown in the sequence, results and Figure 7, despite the abstract's reference to aspartate. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 N179A construct | reported_minimal | UDP-D-xylose formation at 30 min | Keto-product formation decreases and reduced-product formation is minimal. N179 is asparagine, as shown in the sequence, results and Figure 7, despite the abstract's reference to aspartate. | DOI:10.1016/j.jbc.2023.104893
|
| Reported EvdS6 R278A construct | reported_no_significant_change_in | UDP-4-keto-D-xylose formation at 30 min | Figure 7 assigns this result to R278A. However, the Table S1 pair labelled R278A introduces R279A, not R278A, when aligned in the correct orientation to CP058322.1/QLD23489.2. Exact construct identity is unresolved; this edge records the authors' result label, not an independently sequence-verified R278A perturbation. | DOI:10.1016/j.jbc.2023.104893 |
| Reported EvdS6 R278A construct | reported_decreased | UDP-D-xylose formation at 30 min | Figure 7 assigns this result to R278A. However, the Table S1 pair labelled R278A introduces R279A, not R278A, when aligned in the correct orientation to CP058322.1/QLD23489.2. Exact construct identity is unresolved; this edge records the authors' result label, not an independently sequence-verified R278A perturbation. | DOI:10.1016/j.jbc.2023.104893 |
| Reported EvdS6 R279A construct | reported_no_significant_change_in | UDP-4-keto-D-xylose formation at 30 min | Figure 7 assigns this result to R279A. Table S1 has no separately labelled R279A primer pair; the pair labelled R278A encodes R279A against QLD23489.2. The study reports sequencing mutant plasmids, but does not deposit those sequences here. Identity remains review-needed; a changed loop-release mechanism is proposed, not directly measured. | DOI:10.1016/j.jbc.2023.104893 |
| Reported EvdS6 R279A construct | reported_decreased | UDP-D-xylose formation at 30 min | Figure 7 assigns this result to R279A. Table S1 has no separately labelled R279A primer pair; the pair labelled R278A encodes R279A against QLD23489.2. The study reports sequencing mutant plasmids, but does not deposit those sequences here. Identity remains review-needed; a changed loop-release mechanism is proposed, not directly measured. | DOI:10.1016/j.jbc.2023.104893 |
| Native EvdS6 parent | is the wild-type parent of | Reported EvdS6 H87A construct | Reported EvdS6 H87A construct is an engineered point variant of Micromonospora carbonacea subsp. aurantiaca EvdS6 (CP058322.1 HXZ27_04045 / QLD23489.2, 329 aa); the variant node remains ungrounded while anchored to the native parent. | DOI:10.1016/j.jbc.2023.104893 |
| Native EvdS6 parent | is the wild-type parent of | Reported EvdS6 T126A construct | Reported EvdS6 T126A construct is an engineered point variant of Micromonospora carbonacea subsp. aurantiaca EvdS6 (CP058322.1 HXZ27_04045 / QLD23489.2, 329 aa); the variant node remains ungrounded while anchored to the native parent. | DOI:10.1016/j.jbc.2023.104893 |
| Native EvdS6 parent | is the wild-type parent of | Reported EvdS6 E128A construct | Reported EvdS6 E128A construct is an engineered point variant of Micromonospora carbonacea subsp. aurantiaca EvdS6 (CP058322.1 HXZ27_04045 / QLD23489.2, 329 aa); the variant node remains ungrounded while anchored to the native parent. | DOI:10.1016/j.jbc.2023.104893 |
| Native EvdS6 parent | is the wild-type parent of | Reported EvdS6 N179A construct | Reported EvdS6 N179A construct is an engineered point variant of Micromonospora carbonacea subsp. aurantiaca EvdS6 (CP058322.1 HXZ27_04045 / QLD23489.2, 329 aa); the variant node remains ungrounded while anchored to the native parent. | DOI:10.1016/j.jbc.2023.104893 |
| Native EvdS6 parent | is the wild-type parent of | Reported EvdS6 R278A construct | Reported EvdS6 R278A construct is an engineered point variant of Micromonospora carbonacea subsp. aurantiaca EvdS6 (CP058322.1 HXZ27_04045 / QLD23489.2, 329 aa); the variant node remains review_needed while anchored to the native parent. | DOI:10.1016/j.jbc.2023.104893 |
| Native EvdS6 parent | is the wild-type parent of | Reported EvdS6 R279A construct | Reported EvdS6 R279A construct is an engineered point variant of Micromonospora carbonacea subsp. aurantiaca EvdS6 (CP058322.1 HXZ27_04045 / QLD23489.2, 329 aa); the variant node remains review_needed while anchored to the native parent. | DOI:10.1016/j.jbc.2023.104893 |
Every edge carries its own citation; an uncited edge is refused by the corpus tests.
Causal graph — biosynthesis 6 nodes, 5 edges
Native gene-disruption evidence for EvdO1 and EvdMO1 in everninomicin D production. Perturbations, parent proteins and the metabolite readout are separate nodes. No exact reaction order or enzyme-to-ring assignment is inferred from loss of the final products.
| Subject | Predicate | Object | Notes | Evidence |
|---|---|---|---|---|
| Reported evdO1 gene disruption | disrupts_encoding_gene_of | Native EvdO1 parent | The native parent is the 313-aa translation of evdO1/HXZ27_03990, CP058322.1:886309..887250. The deposited 4XBZ construct has this exact core plus a 21-aa N-terminal extension. Gene-name and sequence mapping identifies the parent, not a sequenced deletion allele; the disruption boundaries were not independently checked. | DOI:10.1073/pnas.1500964112 |
| Reported evdO1 gene disruption | abolishes_detectable | Detectable everninomicin D in culture extracts | LC/MS of crude extracts from M. carbonacea var. aurantiaca deletion strains lost detectable everninomicins D-G relative to wild type. Figure 3A includes the D ion at m/z 1534.5 [M-H]-. This is a production readout, not an assay of antibiotic activity or purified-enzyme turnover. No measurable pathway intermediates were identified; the experiment does not assign a particular orthoester linkage or methylenedioxy bridge to this protein. The main text reports PCR/Southern confirmation of double crossovers; the 2015 supplement was not accessible for independent deletion-primer inspection. | DOI:10.1073/pnas.1500964112
|
| Reported evdMO1 gene disruption | disrupts_encoding_gene_of | Native EvdMO1 parent | The native parent is the 450-aa evdMO1/HXZ27_04060 translation at CP058322.1:900465..901817. This is a gene-level perturbation of a fused methyltransferase/oxygenase, not a selective knockout of oxygenase catalysis. It cannot distinguish the two domain functions or exclude indirect/polar effects. The separate 2018 recombinant construct discrepancy does not alter this native reference sequence. | DOI:10.1073/pnas.1500964112 |
| Reported evdMO1 gene disruption | abolishes_detectable | Detectable everninomicin D in culture extracts | LC/MS of crude extracts from M. carbonacea var. aurantiaca deletion strains lost detectable everninomicins D-G relative to wild type. Figure 3A includes the D ion at m/z 1534.5 [M-H]-. This is a production readout, not an assay of antibiotic activity or purified-enzyme turnover. No measurable pathway intermediates were identified; the experiment does not assign a particular orthoester linkage or methylenedioxy bridge to this protein. The main text reports PCR/Southern confirmation of double crossovers; the 2015 supplement was not accessible for independent deletion-primer inspection. | DOI:10.1073/pnas.1500964112
|
| Native EvdO1 parent | has a UniProtKB protein example | EvdO1 (PDB 4XBZ UniProtKB example) | UniProtKB:A0A0M3KL03 (314 aa, derived from PDB 4XBZ) contains one extra N-terminal cloning methionine followed by the complete 313-aa native EvdO1 sequence (CP058322.1 HXZ27_03990 / QLD23479.1); the shorter UniProtKB:A0A1C5AE48 entry (B105_0086, 305 aa) is N-terminally truncated (native residues 9-313). | https://www.uniprot.org/uniprotkb/A0A0M3KL03 |
Every edge carries its own citation; an uncited edge is refused by the corpus tests.
Causal graph — biosynthesis 5 nodes, 4 edges
Recombinant EvdO1/EvdO2 structural observations from catalytically inactive nickel-substituted preparations. EvdO1 is dimeric and EvdO2 monomeric; these are not measurements of native-cell assemblies. Disaccharide docking in the paper is computational, not observed binding or demonstrated biosynthetic turnover.
| Subject | Predicate | Object | Notes | Evidence |
|---|---|---|---|---|
| Crystallized EvdO1 construct | forms_observed_homodimer | Observed recombinant EvdO1 homodimer | 4XBZ contains four dimers in its asymmetric unit, not an octameric biological assembly. UniProt A0A0M3KL03 is a PDB-derived 314-aa sequence: one extra N-terminal methionine followed by native QLD23479.1 (313 aa). It matches the crystallized core including that cloning residue, not an unqualified native sequence. The full deposited 334-aa construct adds the 20-aa MGSSHHHHHHSSGLVPRGSH before the UniProt sequence. No internal mismatch was found. | DOI:10.1073/pnas.1500964112 |
| Observed recombinant EvdO1 homodimer | contains_observed_bound_metal | Substituting nickel(II) | The facial-triad sites contain substituted Ni2+ in 4XBZ. This does not establish nickel as a native cofactor or demonstrate oxygenation activity. | DOI:10.1073/pnas.1500964112 |
| Crystallized EvdO2 | contains_observed_bound_ligand | Bound alpha-ketoglutarate | 4XAC contains bound alpha-ketoglutarate in the nickel-substituted active site. UniProt A0A0M3KL01, the 252-aa QLD23486.1 translation (HXZ27_04030, CP058322.1:895031..895789), and both deposited 4XAB/4XAC polymer sequences are identical. The source organism is M. carbonacea, not the heterologous expression host. Exact native and deposited sequence identity does not establish tag-processing details, which were not independently checked in the inaccessible supplement. Ligand binding does not prove AKG turnover or an exact carbohydrate substrate. | DOI:10.1073/pnas.1500964112 |
| Crystallized EvdO2 | contains_observed_bound_metal | Substituting nickel(II) | 4XAC models Ni2+ rather than Fe2+; the paper deliberately used inactive metal-substituted enzymes for structural work. EvdO2 is monomeric, so no multimeric complex node is assigned. | DOI:10.1073/pnas.1500964112 |
Every edge carries its own citation; an uncited edge is refused by the corpus tests.
Causal graph — biosynthesis 5 nodes, 4 edges
Structural evidence for full-length EvdMO1 and its isolated N-terminal domain EvdMdeltaO1, not a reconstituted methylation/oxygenation pathway. 6EC3 has three molecules in the asymmetric unit but is assigned as monomeric; its affinity-tag contacts are crystal contacts, not a native multienzyme complex. Separate outward-facing active sites suggest independent functions without demonstrating kinetic independence.
| Subject | Predicate | Object | Notes | Evidence |
|---|---|---|---|---|
| Reported full-length EvdMO1 His6 construct | has_experimentally_isolated_n_terminal_domain | Isolated EvdMO1 residues 1-233 His6 construct | QLD28329.2 denotes the native 450-aa parent, HXZ27_04060 at CP058322.1:900465..901817. Its CDS translation matches the deposited 6EC3 core after the 21-aa MGSSHHHHHHSSGLVPRGSHM extension. However, the published reverse primer GCGAAGCTTTCAGGACGGGAGCGTC would encode S447T against this CDS, whereas the deposited sequence retains S447. The unresolved C-terminal model cannot adjudicate this discrepancy; the full-length experimental construct remains REVIEW_NEEDED. The paper names ATCC 27115 genomic DNA and pET28a(+)/E. coli BL21(DE3) expression. PDB-linked UniProt A0A1C5AE13 was not used as an exact parent because it differs at H100N, T219K, A232T and S444A (native-to-UniProt). UniParc UPI0015DCED91 links active EMBL QLD28329.2 and inactive UniProtKB/TrEMBL A0A7H8XVJ8 (450 aa, EvdMO1, taxon 573964) with zero active UniProtKB entries. The domain is a separately expressed truncation, not a demonstrated proteolytic product. Both 5T38 and 5T39 deposit the same 21-aa extension plus native residues 1-233. The published truncation primer inserts TGA after R233, consistent with that endpoint; the residue-447 discrepancy is outside this domain. | DOI:10.1021/acs.biochem.8b00836 |
| Reported full-length EvdMO1 His6 construct | contains_observed_bound_metal | Observed nickel(II) | 6EC3 models nickel acquired during affinity purification, coordinated by H349, D351 and H420; it is not a structure demonstrating native iron catalysis. A histidine from the affinity tag of a crystallographically related molecule also contacts the metal. This crystal contact does not establish a functional protein complex. The full-length construct identity caveat on the domain edge also applies here. | DOI:10.1021/acs.biochem.8b00836 |
| Reported full-length EvdMO1 His6 construct | contains_observed_bound_buffer_ligand | Crystallization-buffer Bis-Tris | Electron density at the expected AKG site in 6EC3 was modeled as Bis-Tris (BTB), a crystallization-buffer component. AKG and an orthosomycin substrate were not modeled there. Do not interpret this observation as an AKG-dependent turnover assay. | DOI:10.1021/acs.biochem.8b00836 |
| Isolated EvdMO1 residues 1-233 His6 construct | contains_observed_bound_ligand | S-adenosylhomocysteine (SAH) | The identifier names the native parent, not the tagged 1-233 fragment. 5T38 was crystallized with 2 mM SAH and resolves bound SAH; the deposited nonpolymer model contains SAH and water, not AKG. The companion 5T39 experiment with 10 mM D-fucose did not resolve fucose density, so no fucose-binding claim is made. Full-length 6EC3 lacks bound SAM/SAH. The proposed E-ring O-methylation assignment is based on AviG5 homology, not demonstrated EvdMO1 turnover. | DOI:10.1021/acs.biochem.8b00836 |
Every edge carries its own citation; an uncited edge is refused by the corpus tests.
Explore across X-Mech
AntibioticMech (everninomicin D) ↗
MediaIngredientMech (naturalproductmech:mibig-22fed17184) ↗
TaxonMech: Micromonospora carbonacea (NCBITaxon:47853) ↗
PathwayMech (mibig:BGC0002085) ↗
Provenance
| Source concept | Source | Version |
|---|---|---|
| BGC0002085 | MIBIG | 3 |
This page is generated from data/natural_products/carbohydrates/everninomicin-d.yaml, which is generated from the committed inventories. Neither is edited by hand.