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mithramycin

CHEBI:31856 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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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.

Structure

Standard InChIKeyCFCUWKMKBJTWLW-BKHRDMLASA-N
SMILESC[C@@H]1[C@H]([C@@H](C[C@@H](O1)O[C@@H]2C[C@@H](O[C@@H]([C@H]2O)C)OC3=CC4=CC5=C(C(=O)[C@H]([C@@H](C5)[C@@H](C(=O)[C@H]([C@@H](C)O)O)OC)O[C@H]6C[C@H]([C@@H]([C@H](O6)C)O)O[C@H]7C[C@H]([C@H]([C@H](O7)C)O)O[C@H]8C[C@]([C@@H]([C@H](O8)C)O)(C)O)C(=C4C(=C3C)O)O)O)O
Stereochemistryfully defined

Filing pathway

Polyketides — 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 pks, 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.

TaxonBasisClusterEvidence
Streptomyces argillaceus
NCBITaxon:41951		 BGC_CHARACTERIZED mibig:BGC0000247 PMID:8654997

Occurrences 8

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:10.1248/CPB.48.575
Streptomyces lividans
NCBITaxon:1916		 LOTUS DOI:10.1007/S00253-017-8642-5
Streptomyces plicatus
NCBITaxon:1922		 CHEBI 10.1016/S1054-3589(08)60218-5
Streptomyces nogalater
NCBITaxon:38314		 LOTUS DOI:10.1039/B200444P
Streptomyces argillaceus
NCBITaxon:41951		 LOTUS DOI:10.1016/0378-1119(96)00029-7
Streptomyces argillaceus
NCBITaxon:41951		 LOTUS DOI:10.1016/J.YMBEN.2013.10.002
Streptomyces argillaceus
NCBITaxon:41951		 LOTUS DOI:10.1021/NP980355K
Streptomyces argillaceus
NCBITaxon:41951		 LOTUS DOI:10.1371/JOURNAL.PONE.0198145

Biosynthetic gene clusters 1

AccessionHostLocus evidenceGenome
mibig:BGC0000247 Streptomyces argillaceus
NCBITaxon:41951 		CLUSTER_DEMONSTRATED genbank:X89899.2

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 MtmW ketoreductase
UniProtKB:Q194Q1		 ungrounded → ungrounded DOI:10.1002/anie.201910241

Step 1: MtmW reduces the MtmOIV-derived mithramycin DK side-chain keto group to iso-mithramycin. Iso-mithramycin then nonenzymatically isomerizes to CHEBI:31856 mithramycin in a Mg2+-catalyzed reaction, so this partial enzymatic step does not set product to the final stereoisomer.

Mechanism & Biosynthesis Overview

PRODUCERS & OCCURRENCE 1 producer (1 causal) 8 cited occurrences BIOSYNTHETIC LOCUS 1 gene cluster 1 curated pathway step NATURAL PRODUCT mithramycin CHEBI:31856 Polyketides TARGETS & BIOACTIVITY 0 molecular targets 0 bioactivities · 7 graphs

Causal graph — biosynthesis 4 nodes, 3 edges

Late Streptomyces argillaceus mithramycin biosynthesis graph for MtmW-catalyzed mithramycin DK reduction to iso-mithramycin and Mg2+-catalyzed isomerization to mithramycin.

SubjectPredicateObjectNotesEvidence
mithramycin DK is reduced by MtmW ketoreductase MtmW reduces the distal keto group of the side chain created by MtmOIV.
DOI:10.1002/anie.201910241
https://mite.lisc.univie.ac.at/repository/MITE0000017
https://www.ncbi.nlm.nih.gov/nuccore/X89899.2
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194Q1
  • reference
    DOI:10.1002/anie.201910241
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmOIV and MtmW catalyze the final two reactions
    notes
    Wheeler et al. showed that MtmOIV and MtmW catalyze the final two enzymatic mithramycin steps: Baeyer-Villiger opening of premithramycin B to mithramycin DK followed by MtmW reduction to iso-mithramycin, which then undergoes Mg2+-catalyzed nonenzymatic isomerization to mithramycin.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000017
    evidence type
    DATABASE_ASSERTION
    snippet
    In vitro assay
    retrieved on
    2026-10-01
    notes
    MITE0000017 is an active MtmW entry for UniProtKB:Q194Q1, GenPept CAK50787.1 and MIBiG BGC0000247. It records NADP-dependent side-chain reduction as a non-intermediate in vitro reaction; the example product SMILES shares the CFCUWKMKBJTWLW connectivity layer with CHEBI:31856.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/X89899.2
    evidence type
    DATABASE_ASSERTION
    snippet
    protein_id="CAK50787.1"
    retrieved on
    2026-10-01
    notes
    GenBank X89899.2 is the Streptomyces argillaceus ATCC 12956 mithramycin cluster sequence and maps mtmW to CAK50787.1.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    protein_id="CAK50787.1"
    retrieved on
    2026-10-01
    notes
    MIBiG BGC0000247.5 places mtmW/CAK50787.1 inside the active Streptomyces argillaceus mithramycin cluster.
  • reference
    https://www.uniprot.org/uniprotkb/Q194Q1
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmW
    retrieved on
    2026-10-01
    notes
    Current unreviewed UniProtKB:Q194Q1 resolves as Streptomyces argillaceus MtmW putative side chain reductase, cross-references EMBL X89899 protein CAK50787.1 and PDB structures 6OVQ, 6OVX and 6OW0, and is sequence-identical to GenPept CAK50787.1.
MtmW ketoreductase forms iso-mithramycin MtmW forms the C2 stereoisomer iso-mithramycin rather than mature mithramycin directly.
DOI:10.1002/anie.201910241
https://mite.lisc.univie.ac.at/repository/MITE0000017
https://www.ncbi.nlm.nih.gov/nuccore/X89899.2
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194Q1
  • reference
    DOI:10.1002/anie.201910241
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmOIV and MtmW catalyze the final two reactions
    notes
    Wheeler et al. showed that MtmOIV and MtmW catalyze the final two enzymatic mithramycin steps: Baeyer-Villiger opening of premithramycin B to mithramycin DK followed by MtmW reduction to iso-mithramycin, which then undergoes Mg2+-catalyzed nonenzymatic isomerization to mithramycin.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000017
    evidence type
    DATABASE_ASSERTION
    snippet
    In vitro assay
    retrieved on
    2026-10-01
    notes
    MITE0000017 is an active MtmW entry for UniProtKB:Q194Q1, GenPept CAK50787.1 and MIBiG BGC0000247. It records NADP-dependent side-chain reduction as a non-intermediate in vitro reaction; the example product SMILES shares the CFCUWKMKBJTWLW connectivity layer with CHEBI:31856.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/X89899.2
    evidence type
    DATABASE_ASSERTION
    snippet
    protein_id="CAK50787.1"
    retrieved on
    2026-10-01
    notes
    GenBank X89899.2 is the Streptomyces argillaceus ATCC 12956 mithramycin cluster sequence and maps mtmW to CAK50787.1.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    protein_id="CAK50787.1"
    retrieved on
    2026-10-01
    notes
    MIBiG BGC0000247.5 places mtmW/CAK50787.1 inside the active Streptomyces argillaceus mithramycin cluster.
  • reference
    https://www.uniprot.org/uniprotkb/Q194Q1
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmW
    retrieved on
    2026-10-01
    notes
    Current unreviewed UniProtKB:Q194Q1 resolves as Streptomyces argillaceus MtmW putative side chain reductase, cross-references EMBL X89899 protein CAK50787.1 and PDB structures 6OVQ, 6OVX and 6OW0, and is sequence-identical to GenPept CAK50787.1.
iso-mithramycin nonenzymatically isomerizes to mithramycin The final isomerization to mithramycin is Mg2+-catalyzed and is not assigned to another biosynthetic protein.
DOI:10.1002/anie.201910241
  • reference
    DOI:10.1002/anie.201910241
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Iso-MTM undergoes a non-enzymatic isomerization to MTM
    notes
    Wheeler et al. showed that MtmOIV and MtmW catalyze the final two enzymatic mithramycin steps: Baeyer-Villiger opening of premithramycin B to mithramycin DK followed by MtmW reduction to iso-mithramycin, which then undergoes Mg2+-catalyzed nonenzymatic isomerization to mithramycin.

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

Causal graph — biosynthesis 4 nodes, 3 edges

Streptomyces argillaceus MtmMI-catalyzed SAM-dependent 4-O-methylation of 4-DPMC to premithramycinone in mithramycin biosynthesis.

SubjectPredicateObjectNotesEvidence
4-demethylpremithramycinone is 4-O-methylated by MtmMI O-methyltransferase MtmMI transfers a SAM-derived methyl group to the C-4 hydroxyl of 4-DPMC in the mithramycin polyketide pathway.
DOI:10.1074/jbc.275.5.3065
https://mite.lisc.univie.ac.at/repository/MITE0000014
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P7
https://www.ncbi.nlm.nih.gov/protein/CAK50791.1
  • reference
    DOI:10.1074/jbc.275.5.3065
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    transfer of tritium from [(3)H]S-adenosylmethionine into 4-DPMC
    notes
    Lozano et al. insertionally inactivated mtmMI and mtmMII and assayed Streptomyces lividans extracts expressing each gene. Extracts from MJM1 expressing mtmMI transferred tritium from [(3)H]S-adenosylmethionine into 4-DPMC, supporting MtmMI as the SAM-dependent 4-O-methyltransferase that converts 4-DPMC toward premithramycinone.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000014
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000014 is active and links MtmMI to UniProtKB:Q194P7, GenPept CAK50791.1, MIBiG BGC0000247, SAM and C-4-O methylation of 4-DPMC to PMC in the mithramycin pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmMI/CAK50791.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as an O-methyltransferase locus.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P7 resolves as a 345 aa Streptomyces argillaceus mtmMI O-methyltransferase entry and cross-references EMBL X89899 protein CAK50791.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50791.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50791.1 is the Streptomyces argillaceus O-methyltransferase encoded by mtmMI and cross-referenced to UniProtKB:Q194P7.
S-adenosyl-L-methionine supplies a methyl group to MtmMI O-methyltransferase The mtmMI heterologous extract assay transferred tritium from radiolabeled S-adenosylmethionine into 4-DPMC.
DOI:10.1074/jbc.275.5.3065
https://mite.lisc.univie.ac.at/repository/MITE0000014
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P7
https://www.ncbi.nlm.nih.gov/protein/CAK50791.1
  • reference
    DOI:10.1074/jbc.275.5.3065
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    transfer of tritium from [(3)H]S-adenosylmethionine into 4-DPMC
    notes
    Lozano et al. insertionally inactivated mtmMI and mtmMII and assayed Streptomyces lividans extracts expressing each gene. Extracts from MJM1 expressing mtmMI transferred tritium from [(3)H]S-adenosylmethionine into 4-DPMC, supporting MtmMI as the SAM-dependent 4-O-methyltransferase that converts 4-DPMC toward premithramycinone.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000014
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000014 is active and links MtmMI to UniProtKB:Q194P7, GenPept CAK50791.1, MIBiG BGC0000247, SAM and C-4-O methylation of 4-DPMC to PMC in the mithramycin pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmMI/CAK50791.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as an O-methyltransferase locus.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P7 resolves as a 345 aa Streptomyces argillaceus mtmMI O-methyltransferase entry and cross-references EMBL X89899 protein CAK50791.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50791.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50791.1 is the Streptomyces argillaceus O-methyltransferase encoded by mtmMI and cross-referenced to UniProtKB:Q194P7.
MtmMI O-methyltransferase forms premithramycinone MITE represents the MtmMI O-methylation as the conversion of 4-DPMC into PMC.
DOI:10.1074/jbc.275.5.3065
https://mite.lisc.univie.ac.at/repository/MITE0000014
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P7
https://www.ncbi.nlm.nih.gov/protein/CAK50791.1
  • reference
    DOI:10.1074/jbc.275.5.3065
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    transfer of tritium from [(3)H]S-adenosylmethionine into 4-DPMC
    notes
    Lozano et al. insertionally inactivated mtmMI and mtmMII and assayed Streptomyces lividans extracts expressing each gene. Extracts from MJM1 expressing mtmMI transferred tritium from [(3)H]S-adenosylmethionine into 4-DPMC, supporting MtmMI as the SAM-dependent 4-O-methyltransferase that converts 4-DPMC toward premithramycinone.
  • reference
    https://mite.lisc.univie.ac.at/repository/MITE0000014
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000014 is active and links MtmMI to UniProtKB:Q194P7, GenPept CAK50791.1, MIBiG BGC0000247, SAM and C-4-O methylation of 4-DPMC to PMC in the mithramycin pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmMI/CAK50791.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as an O-methyltransferase locus.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P7 resolves as a 345 aa Streptomyces argillaceus mtmMI O-methyltransferase entry and cross-references EMBL X89899 protein CAK50791.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50791.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50791.1 is the Streptomyces argillaceus O-methyltransferase encoded by mtmMI and cross-referenced to UniProtKB:Q194P7.

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

Causal graph — biosynthesis 5 nodes, 4 edges

Streptomyces argillaceus MtmMII-catalyzed SAM-dependent C-methylation of a glycosylated mithramycin intermediate.

SubjectPredicateObjectNotesEvidence
MtmMII C-methylation substrate is C-methylated by MtmMII C-methyltransferase MITE represents the MtmMII reaction as C-methylation of a glycosylated mithramycin intermediate; exact local records are absent for the substrate and product structures.
DOI:10.1074/jbc.275.5.3065
DOI:10.1074/jbc.M312351200
https://mite.bioinformatics.nl/repository/MITE0000015
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P8
https://www.ncbi.nlm.nih.gov/protein/CAK50790.1
  • reference
    DOI:10.1074/jbc.275.5.3065
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Characterization of two polyketide methyltransferases involved in the biosynthesis of the antitumor drug mithramycin
    notes
    Lozano et al. characterized Streptomyces argillaceus MtmMI and MtmMII as mithramycin-pathway polyketide methyltransferases; MITE cites this paper for MtmMII in vitro and knock-out support.
  • reference
    DOI:10.1074/jbc.M312351200
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmMII-mediated C-methylation during biosynthesis of the antitumor drug mithramycin
    notes
    Rodriguez et al. analyzed the MtmMII-mediated C-methylation step in mithramycin biosynthesis and its contribution to mithramycin activity and DNA-drug interaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000015
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000015 is active, links MtmMII to UniProtKB:Q194P8, GenPept CAK50790.1 and MIBiG BGC0000247, lists SAM and FeS as cofactors, and represents the reaction as an in vitro- and knock-out-supported C-methylation in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmMII/CAK50790.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a C-methyltransferase locus with a 100% identity MITE0000015 methylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P8 resolves as a 326 aa Streptomyces argillaceus mtmMII C-methyltransferase entry and cross-references EMBL X89899 protein CAK50790.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50790.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50790.1 is the Streptomyces argillaceus C-methyltransferase encoded by mtmMII and cross-referenced to UniProtKB:Q194P8.
S-adenosyl-L-methionine supplies a methyl group to MtmMII C-methyltransferase MITE lists SAM as an MtmMII organic cofactor and UniProt annotates Q194P8 as a SAM-binding methyltransferase.
https://mite.bioinformatics.nl/repository/MITE0000015
https://www.uniprot.org/uniprotkb/Q194P8
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000015
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000015 is active, links MtmMII to UniProtKB:Q194P8, GenPept CAK50790.1 and MIBiG BGC0000247, lists SAM and FeS as cofactors, and represents the reaction as an in vitro- and knock-out-supported C-methylation in the mithramycin biosynthetic pathway.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P8 resolves as a 326 aa Streptomyces argillaceus mtmMII C-methyltransferase entry and cross-references EMBL X89899 protein CAK50790.1.
iron-sulfur cluster serves as cofactor for MtmMII C-methyltransferase MITE lists FeS as an MtmMII inorganic cofactor without specifying the iron-sulfur cluster geometry.
https://mite.bioinformatics.nl/repository/MITE0000015
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000015
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000015 is active, links MtmMII to UniProtKB:Q194P8, GenPept CAK50790.1 and MIBiG BGC0000247, lists SAM and FeS as cofactors, and represents the reaction as an in vitro- and knock-out-supported C-methylation in the mithramycin biosynthetic pathway.
MtmMII C-methyltransferase forms MtmMII C-methylated mithramycin intermediate The MITE reaction product adds an aromatic C-methyl substituent to the submitted mithramycin-pathway substrate structure.
DOI:10.1074/jbc.275.5.3065
DOI:10.1074/jbc.M312351200
https://mite.bioinformatics.nl/repository/MITE0000015
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P8
https://www.ncbi.nlm.nih.gov/protein/CAK50790.1
  • reference
    DOI:10.1074/jbc.275.5.3065
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Characterization of two polyketide methyltransferases involved in the biosynthesis of the antitumor drug mithramycin
    notes
    Lozano et al. characterized Streptomyces argillaceus MtmMI and MtmMII as mithramycin-pathway polyketide methyltransferases; MITE cites this paper for MtmMII in vitro and knock-out support.
  • reference
    DOI:10.1074/jbc.M312351200
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmMII-mediated C-methylation during biosynthesis of the antitumor drug mithramycin
    notes
    Rodriguez et al. analyzed the MtmMII-mediated C-methylation step in mithramycin biosynthesis and its contribution to mithramycin activity and DNA-drug interaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000015
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000015 is active, links MtmMII to UniProtKB:Q194P8, GenPept CAK50790.1 and MIBiG BGC0000247, lists SAM and FeS as cofactors, and represents the reaction as an in vitro- and knock-out-supported C-methylation in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmMII/CAK50790.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a C-methyltransferase locus with a 100% identity MITE0000015 methylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P8 resolves as a 326 aa Streptomyces argillaceus mtmMII C-methyltransferase entry and cross-references EMBL X89899 protein CAK50790.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50790.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50790.1 is the Streptomyces argillaceus C-methyltransferase encoded by mtmMII and cross-referenced to UniProtKB:Q194P8.

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

Causal graph — biosynthesis 4 nodes, 3 edges

Streptomyces argillaceus MtmOIV-catalyzed FAD-dependent oxidative opening and decarboxylation of premithramycin B toward mithramycin DK.

SubjectPredicateObjectNotesEvidence
premithramycin B is oxidatively opened and decarboxylated by MtmOIV Baeyer-Villiger monooxygenase Purified MtmOIV uses premithramycin B as a late-pathway substrate and MITE represents the entry as sequential oxidation and decarboxylation reactions.
DOI:10.1021/ja055750t
DOI:10.1002/anie.201910241
https://mite.bioinformatics.nl/repository/MITE0000016
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P4
https://www.ncbi.nlm.nih.gov/protein/CAK50794.2
  • reference
    DOI:10.1021/ja055750t
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV
    notes
    Gibson et al. assayed purified His6-tagged MtmOIV with premithramycin B, characterized the resulting intermediates and products, and showed that the Streptomyces argillaceus enzyme initiates late mithramycin oxidative ring cleavage as a Baeyer-Villiger monooxygenase.
  • reference
    DOI:10.1002/anie.201910241
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmOIV and MtmW catalyze the final two reactions
    notes
    Wheeler et al. resolved the late handoff in which MtmOIV performs Baeyer-Villiger opening of premithramycin B to mithramycin DK before MtmW reduces that side chain to iso-mithramycin.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000016
    evidence type
    DATABASE_ASSERTION
    snippet
    In vitro assay
    retrieved on
    2026-10-02
    notes
    MITE0000016 is active, links MtmOIV to UniProtKB:Q194P4, GenPept CAK50794.2 and MIBiG BGC0000247, lists FAD as an organic cofactor, and represents three in vitro-supported MtmOIV oxidation and decarboxylation reactions in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000016: Decarboxylation, Oxidation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmOIV/CAK50794.2 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as an oxygenase locus with a 100% identity MITE0000016 decarboxylation/oxidation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P4
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmOIV
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P4 resolves as a 533 aa Streptomyces argillaceus mtmOIV oxygenase entry, cross-references EMBL X89899 protein CAK50794.2 and FAD-bound PDB structures, and is sequence-identical to GenPept CAK50794.2.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50794.2
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194P4
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50794.2 is the 533 aa Streptomyces argillaceus protein encoded by mtmOIV and cross-referenced to UniProtKB:Q194P4.
FAD serves as cofactor for MtmOIV Baeyer-Villiger monooxygenase MITE lists FAD as an MtmOIV organic cofactor and UniProt maps Q194P4 to FAD-bound PDB structures.
https://mite.bioinformatics.nl/repository/MITE0000016
https://www.uniprot.org/uniprotkb/Q194P4
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000016
    evidence type
    DATABASE_ASSERTION
    snippet
    In vitro assay
    retrieved on
    2026-10-02
    notes
    MITE0000016 is active, links MtmOIV to UniProtKB:Q194P4, GenPept CAK50794.2 and MIBiG BGC0000247, lists FAD as an organic cofactor, and represents three in vitro-supported MtmOIV oxidation and decarboxylation reactions in the mithramycin biosynthetic pathway.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P4
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmOIV
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P4 resolves as a 533 aa Streptomyces argillaceus mtmOIV oxygenase entry, cross-references EMBL X89899 protein CAK50794.2 and FAD-bound PDB structures, and is sequence-identical to GenPept CAK50794.2.
MtmOIV Baeyer-Villiger monooxygenase forms mithramycin DK MtmOIV generates the mithramycin DK side chain that is subsequently reduced by MtmW in the final enzymatic mithramycin step.
DOI:10.1021/ja055750t
DOI:10.1002/anie.201910241
https://mite.bioinformatics.nl/repository/MITE0000016
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P4
https://www.ncbi.nlm.nih.gov/protein/CAK50794.2
  • reference
    DOI:10.1021/ja055750t
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV
    notes
    Gibson et al. assayed purified His6-tagged MtmOIV with premithramycin B, characterized the resulting intermediates and products, and showed that the Streptomyces argillaceus enzyme initiates late mithramycin oxidative ring cleavage as a Baeyer-Villiger monooxygenase.
  • reference
    DOI:10.1002/anie.201910241
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmOIV and MtmW catalyze the final two reactions
    notes
    Wheeler et al. resolved the late handoff in which MtmOIV performs Baeyer-Villiger opening of premithramycin B to mithramycin DK before MtmW reduces that side chain to iso-mithramycin.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000016
    evidence type
    DATABASE_ASSERTION
    snippet
    In vitro assay
    retrieved on
    2026-10-02
    notes
    MITE0000016 is active, links MtmOIV to UniProtKB:Q194P4, GenPept CAK50794.2 and MIBiG BGC0000247, lists FAD as an organic cofactor, and represents three in vitro-supported MtmOIV oxidation and decarboxylation reactions in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000016: Decarboxylation, Oxidation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmOIV/CAK50794.2 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as an oxygenase locus with a 100% identity MITE0000016 decarboxylation/oxidation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P4
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmOIV
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P4 resolves as a 533 aa Streptomyces argillaceus mtmOIV oxygenase entry, cross-references EMBL X89899 protein CAK50794.2 and FAD-bound PDB structures, and is sequence-identical to GenPept CAK50794.2.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50794.2
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194P4
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50794.2 is the 533 aa Streptomyces argillaceus protein encoded by mtmOIV and cross-referenced to UniProtKB:Q194P4.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Streptomyces argillaceus MtmGIV-catalyzed glycosylation reactions in mithramycin deoxysugar assembly.

SubjectPredicateObjectNotesEvidence
MtmGIV glycosylation substrate is glycosylated by MtmGIV glycosyltransferase MITE represents MtmGIV as a glycosyltransferase for two mithramycin intermediates; exact local records are absent for the submitted substrate and product structures.
DOI:10.1007/PL00008667
DOI:10.1002/anie.201205414
https://mite.bioinformatics.nl/repository/MITE0000018
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194Q0
https://www.ncbi.nlm.nih.gov/protein/CAK50788.1
  • reference
    DOI:10.1007/PL00008667
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Characterization of two glycosyltransferases involved in early glycosylation steps
    notes
    Blanco et al. characterized Streptomyces argillaceus glycosyltransferases involved in early mithramycin glycosylation; MITE cites this paper for the knock-out-supported MtmGIV glycosylation reaction.
  • reference
    DOI:10.1002/anie.201205414
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Cooperation of Two Bifunctional Enzymes in the Biosynthesis and Attachment of Deoxysugars
    notes
    Wang et al. assayed mithramycin deoxysugar biosynthesis and attachment by bifunctional enzymes; MITE cites this paper for an in vitro MtmGIV glycosylation reaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000018
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000018 is active, links MtmGIV to UniProtKB:Q194Q0, GenPept CAK50788.1 and MIBiG BGC0000247, and represents one in vitro-supported and one knock-out-supported MtmGIV glycosylation reaction in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000018: Glycosylation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmGIV/CAK50788.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a glycosyltransferase locus with a 100% identity MITE0000018 glycosylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194Q0
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmGIV
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194Q0 resolves as a 407 aa Streptomyces argillaceus mtmGIV glycosyltransferase entry and cross-references EMBL X89899 protein CAK50788.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50788.1
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194Q0
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50788.1 is the 407 aa Streptomyces argillaceus glycosyltransferase encoded by mtmGIV and cross-referenced to UniProtKB:Q194Q0.
MtmGIV glycosyltransferase forms MtmGIV-glycosylated mithramycin intermediate The MITE MtmGIV reactions add deoxysugar moieties to mithramycin-pathway acceptor structures.
DOI:10.1007/PL00008667
DOI:10.1002/anie.201205414
https://mite.bioinformatics.nl/repository/MITE0000018
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194Q0
https://www.ncbi.nlm.nih.gov/protein/CAK50788.1
  • reference
    DOI:10.1007/PL00008667
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Characterization of two glycosyltransferases involved in early glycosylation steps
    notes
    Blanco et al. characterized Streptomyces argillaceus glycosyltransferases involved in early mithramycin glycosylation; MITE cites this paper for the knock-out-supported MtmGIV glycosylation reaction.
  • reference
    DOI:10.1002/anie.201205414
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    Cooperation of Two Bifunctional Enzymes in the Biosynthesis and Attachment of Deoxysugars
    notes
    Wang et al. assayed mithramycin deoxysugar biosynthesis and attachment by bifunctional enzymes; MITE cites this paper for an in vitro MtmGIV glycosylation reaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000018
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000018 is active, links MtmGIV to UniProtKB:Q194Q0, GenPept CAK50788.1 and MIBiG BGC0000247, and represents one in vitro-supported and one knock-out-supported MtmGIV glycosylation reaction in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000018: Glycosylation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmGIV/CAK50788.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a glycosyltransferase locus with a 100% identity MITE0000018 glycosylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194Q0
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmGIV
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194Q0 resolves as a 407 aa Streptomyces argillaceus mtmGIV glycosyltransferase entry and cross-references EMBL X89899 protein CAK50788.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50788.1
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194Q0
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50788.1 is the 407 aa Streptomyces argillaceus glycosyltransferase encoded by mtmGIV and cross-referenced to UniProtKB:Q194Q0.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Streptomyces argillaceus MtmGIII-catalyzed glycosylation in mithramycin deoxysugar assembly.

SubjectPredicateObjectNotesEvidence
MtmGIII glycosylation substrate is glycosylated by MtmGIII glycosyltransferase MITE represents MtmGIII as a glycosyltransferase for a mithramycin intermediate; an exact local record is absent for the submitted substrate structure.
DOI:10.1007/PL00008667
https://mite.bioinformatics.nl/repository/MITE0000019
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P9
https://www.ncbi.nlm.nih.gov/protein/CAK50789.1
  • reference
    DOI:10.1007/PL00008667
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmGIV and MtmGIII catalyze the first two glycosylation steps in mithramycin biosynthesis
    notes
    Blanco et al. used independent insertional inactivation of mtmGIII and mtmGIV to demonstrate early Streptomyces argillaceus mithramycin glycosylation roles; MITE cites this paper for the knock-out-supported MtmGIII glycosylation reaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000019
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000019 is active, links MtmGIII to UniProtKB:Q194P9, GenPept CAK50789.1 and MIBiG BGC0000247, and represents a knock-out-supported MtmGIII glycosylation reaction in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000019: Glycosylation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmGIII/CAK50789.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a glycosyltransferase locus with a 100% identity MITE0000019 glycosylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P9
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmGIII
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P9 resolves as a 396 aa Streptomyces argillaceus mtmGIII glycosyltransferase entry and cross-references EMBL X89899 protein CAK50789.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50789.1
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194P9
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50789.1 is the 396 aa Streptomyces argillaceus glycosyltransferase encoded by mtmGIII and cross-referenced to UniProtKB:Q194P9.
MtmGIII glycosyltransferase forms MtmGIII-glycosylated mithramycin intermediate The MITE MtmGIII reaction adds a deoxysugar moiety to a mithramycin-pathway acceptor structure.
DOI:10.1007/PL00008667
https://mite.bioinformatics.nl/repository/MITE0000019
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P9
https://www.ncbi.nlm.nih.gov/protein/CAK50789.1
  • reference
    DOI:10.1007/PL00008667
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    MtmGIV and MtmGIII catalyze the first two glycosylation steps in mithramycin biosynthesis
    notes
    Blanco et al. used independent insertional inactivation of mtmGIII and mtmGIV to demonstrate early Streptomyces argillaceus mithramycin glycosylation roles; MITE cites this paper for the knock-out-supported MtmGIII glycosylation reaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000019
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000019 is active, links MtmGIII to UniProtKB:Q194P9, GenPept CAK50789.1 and MIBiG BGC0000247, and represents a knock-out-supported MtmGIII glycosylation reaction in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000019: Glycosylation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmGIII/CAK50789.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a glycosyltransferase locus with a 100% identity MITE0000019 glycosylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P9
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmGIII
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P9 resolves as a 396 aa Streptomyces argillaceus mtmGIII glycosyltransferase entry and cross-references EMBL X89899 protein CAK50789.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50789.1
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194P9
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50789.1 is the 396 aa Streptomyces argillaceus glycosyltransferase encoded by mtmGIII and cross-referenced to UniProtKB:Q194P9.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Streptomyces argillaceus MtmGII-catalyzed glycosylation in mithramycin deoxysugar assembly.

SubjectPredicateObjectNotesEvidence
MtmGII glycosylation substrate is glycosylated by MtmGII glycosyltransferase MITE represents MtmGII as a glycosyltransferase for a mithramycin intermediate; an exact local record is absent for the submitted substrate structure.
DOI:10.1002/cbic.200400309
https://mite.bioinformatics.nl/repository/MITE0000020
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P6
https://www.ncbi.nlm.nih.gov/protein/CAK50792.1
  • reference
    DOI:10.1002/cbic.200400309
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    3A-deolivosylpremithramycin B and its conversion to premithramycin B by glycosyltransferase MtmGII
    notes
    Nur-e-Alam et al. elucidated a late Streptomyces argillaceus mithramycin glycosylation step mediated by MtmGII; MITE cites this paper for the knock-out-supported MtmGII glycosylation reaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000020
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000020 is active, links MtmGII to UniProtKB:Q194P6, GenPept CAK50792.1 and MIBiG BGC0000247, and represents a knock-out-supported MtmGII glycosylation reaction in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000020: Glycosylation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmGII/CAK50792.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a glycosyltransferase locus with a 100% identity MITE0000020 glycosylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P6
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmGII
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P6 resolves as a 379 aa Streptomyces argillaceus mtmGII glycosyltransferase entry and cross-references EMBL X89899 protein CAK50792.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50792.1
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194P6
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50792.1 is the 379 aa Streptomyces argillaceus glycosyltransferase encoded by mtmGII and cross-referenced to UniProtKB:Q194P6.
MtmGII glycosyltransferase forms MtmGII-glycosylated mithramycin intermediate The MITE MtmGII reaction adds a deoxysugar moiety to a mithramycin-pathway acceptor structure.
DOI:10.1002/cbic.200400309
https://mite.bioinformatics.nl/repository/MITE0000020
https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
https://www.uniprot.org/uniprotkb/Q194P6
https://www.ncbi.nlm.nih.gov/protein/CAK50792.1
  • reference
    DOI:10.1002/cbic.200400309
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    3A-deolivosylpremithramycin B and its conversion to premithramycin B by glycosyltransferase MtmGII
    notes
    Nur-e-Alam et al. elucidated a late Streptomyces argillaceus mithramycin glycosylation step mediated by MtmGII; MITE cites this paper for the knock-out-supported MtmGII glycosylation reaction.
  • reference
    https://mite.bioinformatics.nl/repository/MITE0000020
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-02
    notes
    MITE0000020 is active, links MtmGII to UniProtKB:Q194P6, GenPept CAK50792.1 and MIBiG BGC0000247, and represents a knock-out-supported MtmGII glycosylation reaction in the mithramycin biosynthetic pathway.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000247.5/BGC0000247.gbk
    evidence type
    DATABASE_ASSERTION
    snippet
    MITE0000020: Glycosylation (100% identity)
    retrieved on
    2026-10-02
    notes
    MIBiG BGC0000247.5 places mtmGII/CAK50792.1 inside the active Streptomyces argillaceus mithramycin biosynthetic gene cluster as a glycosyltransferase locus with a 100% identity MITE0000020 glycosylation annotation.
  • reference
    https://www.uniprot.org/uniprotkb/Q194P6
    evidence type
    DATABASE_ASSERTION
    snippet
    GN=mtmGII
    retrieved on
    2026-10-02
    notes
    Current UniProtKB:Q194P6 resolves as a 379 aa Streptomyces argillaceus mtmGII glycosyltransferase entry and cross-references EMBL X89899 protein CAK50792.1.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAK50792.1
    evidence type
    DATABASE_ASSERTION
    snippet
    UniProtKB/TrEMBL:Q194P6
    retrieved on
    2026-10-02
    notes
    NCBI Protein CAK50792.1 is the 379 aa Streptomyces argillaceus glycosyltransferase encoded by mtmGII and cross-referenced to UniProtKB:Q194P6.

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

Elsewhere in the fleet

Explore across X-Mech

AntibioticMech (mithramycin) ↗ MediaIngredientMech (CHEBI:31856) ↗ TaxonMech: Streptomyces argillaceus (NCBITaxon:41951) ↗ PathwayMech (mibig:BGC0000247) ↗

Provenance

Source conceptSourceVersion
BGC0000247MIBIG5
CHEBI:31856CHEBI3-star

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