deferrichrome

CHEBI:90132 EXACT REVIEWED

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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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

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A homodetic cyclic peptide composed from two units of three glycyl and three N5-acetyl-N5-hydroxy-L-ornithyl residues.

Structure

Standard InChIKey	ZFDAUYPBCXMSBF-ACRUOGEOSA-N
SMILES	CC(=O)N(O)CCC[C@@H]1NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](CCCN(O)C(C)=O)NC(=O)[C@H](CCCN(O)C(C)=O)NC1=O
Stereochemistry	fully defined

Filing pathway

Amino acids and peptides — computed by NPClassifier npclassifier.gnps2.org@2026-10-31, which is why it is pinned rather than recomputed.

Producer organisms 3

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	Evidence
Ustilago maydis Strain: 518 NCBITaxon:5270	BGC_CHARACTERIZED	PMID:8430103 reference PMID:8430103 evidence type PRIMARY_EXPERIMENT notes Cloning, targeted disruption, and complementation of sid1 (L-ornithine N5-oxygenase) in Ustilago maydis establish biosynthesis of the cyclic hexapeptide trihydroxamate siderophore deferrichrome.
Ustilago maydis Strain: FB1 NCBITaxon:5270	BGC_CHARACTERIZED	PMID:11395469 reference PMID:11395469 evidence type PRIMARY_EXPERIMENT notes Targeted gene replacement of sid2 (nonribosomal peptide synthetase) in Ustilago maydis completely abolishes deferrichrome biosynthesis.
Schizosaccharomyces pombe Strain: 972h- NCBITaxon:4896	BGC_CHARACTERIZED	PMID:20435771 reference PMID:20435771 evidence type PRIMARY_EXPERIMENT notes Genetic deletion of sib1+ (NRPS) and sib2+ (L-ornithine N5-oxygenase) in Schizosaccharomyces pombe demonstrates biosynthesis of ferrichrome/deferrichrome.

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
Mus musculus NCBITaxon:10090	CHEBI	https://www.ebi.ac.uk/chebi/CHEBI:90132

Biosynthesis curated

Written by a curator with claim-level evidence on each step; not derived from a source. This is what the rest of the record exists to support.

Step	Enzyme	Reaction	Substrate → product	Evidence
1	L-ornithine N5-monooxygenase (Sid1 / Sib2)		CHEBI:15729 → CHEBI:79095	PMID:8430103
2	N5-hydroxyornithine N5-acetyltransferase (Sib3) and ferrichrome nonribosomal peptide synthetase (Sid2 / Sib1)		CHEBI:79095 + CHEBI:15351 + CHEBI:15428 + CHEBI:15422 → CHEBI:90132	PMID:11395469

Step 1: FAD- and NADPH-dependent N5-hydroxylation of L-ornithine to N(5)-hydroxy-L-ornithine by Sid1 (Ustilago maydis) or Sib2 (Schizosaccharomyces pombe).

Step 2: Acetyl-CoA-dependent N5-acetylation of N(5)-hydroxy-L-ornithine (by Sib3 in S. pombe) followed by iterative assembly and macrocyclization of three glycine units and three N5-acetyl-N5-hydroxy-L-ornithine units by the multimodular NRPS Sid2 (Ustilago maydis) or Sib1 (Schizosaccharomyces pombe) to release deferrichrome.

Mechanism & Biosynthesis Overview

Causal graph — bioactivity 11 nodes, 10 edges

Fungal NRPS-directed biosynthesis of the cyclic hexapeptide trihydroxamate siderophore deferrichrome via Sid1/Sid2 (Ustilago maydis) and Sib1/Sib2/Sib3 (Schizosaccharomyces pombe), octahedral chelation of Fe(III) and CMM cations Ga(III) and Al(III), and xenosiderophore uptake via bacterial FhuA.

Subject	Predicate	Object	Notes	Evidence
L-ornithine	substrate_of	L-ornithine N5-monooxygenase Sid1	Sid1/Sib2 catalyzes N5-hydroxylation of L-ornithine.	PMID:8430103 reference PMID:8430103 evidence type PRIMARY_EXPERIMENT notes sid1 encodes L-ornithine N5-oxygenase in Ustilago maydis.
L-ornithine N5-monooxygenase Sid1	synthesizes	N(5)-hydroxy-L-ornithine	Produces N(5)-hydroxy-L-ornithine.	PMID:8430103 reference PMID:8430103 evidence type PRIMARY_EXPERIMENT notes Sid1 catalyzes N5-hydroxylation of L-ornithine to N(5)-hydroxy-L-ornithine.
N(5)-hydroxy-L-ornithine	substrate_of	Ferrichrome synthetase Sid2 / Sib1	Following N5-acetylation by Sib3, three N(5)-hydroxy-L-ornithine-derived hydroxamate units are incorporated by the NRPS.	PMID:11395469 PMID:35928155 reference PMID:11395469 evidence type PRIMARY_EXPERIMENT notes Sid2 NRPS incorporates three hydroxamate-ornithine units and three glycines. reference PMID:35928155 evidence type PRIMARY_EXPERIMENT notes Sib3 N5-acetylates N(5)-hydroxy-L-ornithine prior to NRPS assembly.
glycine	substrate_of	Ferrichrome synthetase Sid2 / Sib1	Three glycine residues form the tripeptide spacer of the hexapeptide ring.	PMID:20435771 reference PMID:20435771 evidence type PRIMARY_EXPERIMENT notes Sib1 NRPS condenses glycine and N5-acetyl-N5-hydroxyornithine into ferrichrome.
Ferrichrome synthetase Sid2 / Sib1	synthesizes	deferrichrome	Macrocyclization releases metal-free deferrichrome.	PMID:11395469 reference PMID:11395469 evidence type PRIMARY_EXPERIMENT notes Disruption of sid2 abolishes deferrichrome production.
deferrichrome	chelates	iron(3+)	Hexadentate trihydroxamate chelation of Fe(III) (log beta110 = 29.1).	PMID:9856937 reference PMID:9856937 evidence type PRIMARY_EXPERIMENT notes Octahedral coordination of Fe(III) in ferrichrome.
deferrichrome	chelates	gallium(3+)	[CMM] Octahedral chelation of trivalent gallium(3+) to form gallichrome.	PMID:10742172 reference PMID:10742172 evidence type PRIMARY_EXPERIMENT notes 1.9 A crystal structure of gallichrome bound to E. coli FhuD.
deferrichrome	chelates	aluminium(3+)	[CMM] Octahedral chelation of trivalent aluminium(3+) to form alumichrome.	PMID:2279065 reference PMID:2279065 evidence type PRIMARY_EXPERIMENT notes 1H-NMR solution conformation of alumichrome.
deferrichrome	binds	Ferrichrome outer membrane transporter FhuA	In its ferric-complexed form (ferrichrome), deferrichrome binds the extracellular pocket of the E. coli outer membrane transporter FhuA.	PMID:9856937 reference PMID:9856937 evidence type PRIMARY_EXPERIMENT notes Crystal structure of FhuA bound to ferrichrome.
Ferrichrome outer membrane transporter FhuA	enables	siderophore transport	TonB-dependent translocation of ferrichrome into the periplasm.	PMID:9856937 reference PMID:9856937 evidence type PRIMARY_EXPERIMENT notes Ligand binding induces allosteric unwinding of the FhuA TonB box.

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

Molecular targets 3

Target	Target organism	Measurement	Evidence
iron(3+) OTHER BINDS Hexadentate octahedral coordination of ferric iron(3+) via three N5-acetyl-N5-hydroxy-L-ornithine hydroxamate groups on the cyclic hexapeptide cyclo[(Gly)3-(N5-acetyl-N5-hydroxy-L-Orn)3] scaffold to form ferrichrome (log beta110 = 29.1).			PMID:8430103 PMID:9856937 reference PMID:8430103 evidence type PRIMARY_EXPERIMENT notes Biosynthesis of the cyclic hexapeptide trihydroxamate siderophore ferrichrome (deferrichrome + Fe(III)) in Ustilago maydis. reference PMID:9856937 evidence type PRIMARY_EXPERIMENT notes X-ray crystal structure of ferric-bound ferrichrome complexed with the Escherichia coli outer membrane transporter FhuA at 2.5 A resolution.
gallium(3+) OTHER BINDS [Critical Mineral & Material (CMM)] High-affinity octahedral chelation of trivalent gallium(3+) by deferrichrome to form [Ga(III)]-deferrichrome (gallichrome), characterized by 1H-NMR solution conformation analysis, a 1.9 A co-crystal structure with Escherichia coli FhuD, and 68Ga-radiolabeled PET imaging.			PMID:10742172 PMID:2279065 PMID:38436776 reference PMID:10742172 evidence type PRIMARY_EXPERIMENT notes 1.9 A X-ray crystal structure of Escherichia coli periplasmic binding protein FhuD complexed with gallichrome ([Ga(III)]-deferrichrome). reference PMID:2279065 evidence type PRIMARY_EXPERIMENT notes 1H-NMR spectroscopic determination of the solution conformation of gallichrome ([Ga(III)]-deferrichrome). reference PMID:38436776 evidence type PRIMARY_EXPERIMENT notes Preclinical characterization of 68Ga-labeled ferrichrome siderophore complexes for PET imaging.
aluminium(3+) OTHER BINDS [Critical Mineral & Material (CMM)] Octahedral coordination of trivalent aluminium(3+) by deferrichrome to form the diamagnetic complex alumichrome ([Al(III)]-deferrichrome), characterized by 1H-, 13C-, and 15N-NMR spectroscopy.			PMID:2279065 PMID:486399 reference PMID:2279065 evidence type PRIMARY_EXPERIMENT notes 1H-NMR solution conformation analysis of alumichrome ([Al(III)]-deferrichrome) in d6-DMSO. reference PMID:486399 evidence type PRIMARY_EXPERIMENT notes Complete 13C-NMR chemical shift assignment and conformational analysis of alumichrome.

Explore across X-Mech

AntibioticMech (deferrichrome) ↗ MediaIngredientMech (CHEBI:90132) ↗ TaxonMech: Ustilago maydis (NCBITaxon:5270) ↗ TaxonMech: Ustilago maydis (NCBITaxon:5270) ↗ TaxonMech: Schizosaccharomyces pombe (NCBITaxon:4896) ↗

Provenance

Source concept	Source	Version
CHEBI:90132	CHEBI	3-star

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