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staphyloferrin B

CHEBI:134612 EXACT SEEDED

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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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 siderophore composed from L-2,3-diaminopropionic acid, citric acid, 1,2-diaminoethane and α-ketoglutaric acid units.

Structure

Standard InChIKeySIAZVTIHOHTZDD-PWJLMRLQSA-N
SMILESC(CC(=O)NCCNC(=O)C[C@](CC(=O)NC[C@@H](C(=O)O)N)(C(=O)O)O)C(=O)C(=O)O
Stereochemistryfully defined
Cross-referencesnpatlas:NPA012996

Filing pathway

Amino acids and peptides — 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 other, 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
Staphylococcus aureus subsp. aureus NCTC 8325
NCBITaxon:93061		 SOURCE_ASSERTION mibig:BGC0000943 PMID:14688077

Occurrences 4

Somebody found the compound in this organism and cited it. That is not a claim that the organism makes it, and nothing here promotes one to the other.

TaxonSourceReference
Cupriavidus necator
NCBITaxon:106590		 LOTUS DOI:10.1515/ZNC-1999-1103
Staphylococcus aureus
NCBITaxon:1280		 CHEBI PMID:26030732
Staphylococcus hyicus
NCBITaxon:1284		 LOTUS DOI:10.1016/0378-1097(94)90002-7
Staphylococcus hyicus
NCBITaxon:1284		 CHEBI PMID:8138126

Biosynthetic gene clusters 1

AccessionHostLocus evidenceGenome
mibig:BGC0000943 Staphylococcus aureus subsp. aureus NCTC 8325
NCBITaxon:93061 		CLUSTER_DEMONSTRATED genbank:LS483365.1

A locus claim and a taxon claim are different questions. Heterologous expression settles the first and leaves the second where the isolation report left it.

Biosynthesis curated

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

StepEnzymeReactionSubstrate → productEvidence
1 SbnE (NCTC 8325 reference)
UniProtKB:Q2G1M9		 RHEA:59124 CHEBI:57721 + CHEBI:16947 → CHEBI:142969 https://www.uniprot.org/uniprotkb/Q2G1M9
2 SbnH (NCTC 8325 reference)
UniProtKB:Q2G1M6		 RHEA:59120 CHEBI:142969 → CHEBI:142970 https://www.uniprot.org/uniprotkb/Q2G1M6
3 SbnF (NCTC 8325 reference)
UniProtKB:Q2G1M8		 RHEA:59128 CHEBI:142970 + CHEBI:57721 → CHEBI:142971 https://www.uniprot.org/uniprotkb/Q2G1M8
4 Staphyloferrin B synthase
UniProtKB:Q2G1N1		 RHEA:59132 CHEBI:142971 + CHEBI:16810 → CHEBI:134612 DOI:10.1111/j.1365-2958.2009.06880.x

Step 1: ATP-dependent condensation of L-Dap and citrate forms citryl-L-Dap, AMP and diphosphate; assembly step 1. This is the database-assigned assembly order, not inferred gene order; I/A/B precursor synthesis is represented separately without invented step numbers. The LS483365 reference matches the UniProt sequence.

Step 2: Decarboxylation of citryl-L-Dap with a proton forms citryl-diaminoethane and carbon dioxide; assembly step 2. This is the database-assigned assembly order, not inferred gene order; I/A/B precursor synthesis is represented separately without invented step numbers. The LS483365 reference matches the UniProt sequence.

Step 3: ATP-dependent condensation of citryl-diaminoethane and L-Dap forms the SbnC acceptor, AMP and diphosphate; assembly step 3. This is the database-assigned assembly order, not inferred gene order; I/A/B precursor synthesis is represented separately without invented step numbers. The 616-aa CP000253 reference is selected; the 592-aa LS483365 model is not treated as the same protein.

Step 4: Staphylococcus aureus NCTC 8325 SbnC catalyzes the ATP-dependent terminal condensation of the SbnF product with 2-oxoglutarate to form staphyloferrin B. RHEA:59132 uses the staphyloferrin B(2-) participant CHEBI:136993; this record denotes neutral CHEBI:134612 with the same stereochemistry.

Mechanism & Biosynthesis Overview

PRODUCERS & OCCURRENCE 1 producer (0 causal) 4 cited occurrences BIOSYNTHETIC LOCUS 1 gene cluster 4 curated pathway steps NATURAL PRODUCT staphyloferrin B CHEBI:134612 Amino acids and peptides TARGETS & BIOACTIVITY 0 molecular targets 0 bioactivities · 5 graphs

Causal graph — biosynthesis 4 nodes, 3 edges

Staphylococcus aureus NCTC 8325 SbnC-catalyzed terminal condensation of 2-oxoglutarate with the SbnF product in staphyloferrin B biosynthesis.

SubjectPredicateObjectNotesEvidence
2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate is condensed with 2-oxoglutarate by SbnC RHEA:59132 represents this acceptor as the CHEBI:142971 product of the preceding SbnF synthetase reaction.
DOI:10.1111/j.1365-2958.2009.06880.x
https://mibig.secondarymetabolites.org/repository/BGC0000943.5/
RHEA:59132
https://www.uniprot.org/uniprotkb/Q2G1N1
  • reference
    DOI:10.1111/j.1365-2958.2009.06880.x
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    SbnC activates α-KG in a reaction that completes the synthesis of staphyloferrin B
    notes
    Cheung et al. reconstituted staphyloferrin B biosynthesis in vitro with purified recombinant Sbn enzymes and assigned SbnC as the final synthetase that condenses 2-oxoglutarate with the SbnF product.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000943.5/
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    MIBiG entry version 5 links BGC0000943 to staphyloferrin B biosynthesis in Staphylococcus aureus subsp. aureus NCTC 8325 and lists the LS483365.1 sbnC gene as NCTC8325_00067/SQF72447.1.
  • reference
    RHEA:59132
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    RHEA:59132 annotates EC:6.3.2.56 as 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate, 2-oxoglutarate, and ATP forming staphyloferrin B, AMP, diphosphate, and a proton.
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    Reviewed UniProtKB:Q2G1N1 is the Staphylococcus aureus NCTC 8325 / PS 47 SbnC staphyloferrin B synthase, ordered locus SAOUHSC_00077, and annotates RHEA:59132.
2-oxoglutarate is ligated to the SbnC acceptor by SbnC RHEA:59132 consumes ATP and releases AMP, diphosphate, and a proton.
DOI:10.1111/j.1365-2958.2009.06880.x
https://mibig.secondarymetabolites.org/repository/BGC0000943.5/
RHEA:59132
https://www.uniprot.org/uniprotkb/Q2G1N1
  • reference
    DOI:10.1111/j.1365-2958.2009.06880.x
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    SbnC activates α-KG in a reaction that completes the synthesis of staphyloferrin B
    notes
    Cheung et al. reconstituted staphyloferrin B biosynthesis in vitro with purified recombinant Sbn enzymes and assigned SbnC as the final synthetase that condenses 2-oxoglutarate with the SbnF product.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000943.5/
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    MIBiG entry version 5 links BGC0000943 to staphyloferrin B biosynthesis in Staphylococcus aureus subsp. aureus NCTC 8325 and lists the LS483365.1 sbnC gene as NCTC8325_00067/SQF72447.1.
  • reference
    RHEA:59132
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    RHEA:59132 annotates EC:6.3.2.56 as 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate, 2-oxoglutarate, and ATP forming staphyloferrin B, AMP, diphosphate, and a proton.
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    Reviewed UniProtKB:Q2G1N1 is the Staphylococcus aureus NCTC 8325 / PS 47 SbnC staphyloferrin B synthase, ordered locus SAOUHSC_00077, and annotates RHEA:59132.
SbnC forms staphyloferrin B RHEA uses staphyloferrin B(2-) CHEBI:136993 as the product participant; this graph points at neutral CHEBI:134612, the exact structure recorded for BGC0000943.
DOI:10.1111/j.1365-2958.2009.06880.x
https://mibig.secondarymetabolites.org/repository/BGC0000943.5/
RHEA:59132
https://www.uniprot.org/uniprotkb/Q2G1N1
  • reference
    DOI:10.1111/j.1365-2958.2009.06880.x
    evidence type
    PRIMARY_EXPERIMENT
    snippet
    SbnC activates α-KG in a reaction that completes the synthesis of staphyloferrin B
    notes
    Cheung et al. reconstituted staphyloferrin B biosynthesis in vitro with purified recombinant Sbn enzymes and assigned SbnC as the final synthetase that condenses 2-oxoglutarate with the SbnF product.
  • reference
    https://mibig.secondarymetabolites.org/repository/BGC0000943.5/
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    MIBiG entry version 5 links BGC0000943 to staphyloferrin B biosynthesis in Staphylococcus aureus subsp. aureus NCTC 8325 and lists the LS483365.1 sbnC gene as NCTC8325_00067/SQF72447.1.
  • reference
    RHEA:59132
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    RHEA:59132 annotates EC:6.3.2.56 as 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate, 2-oxoglutarate, and ATP forming staphyloferrin B, AMP, diphosphate, and a proton.
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-09-30
    notes
    Reviewed UniProtKB:Q2G1N1 is the Staphylococcus aureus NCTC 8325 / PS 47 SbnC staphyloferrin B synthase, ordered locus SAOUHSC_00077, and annotates RHEA:59132.

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

Causal graph — biosynthesis 9 nodes, 8 edges

Database-qualified L-Dap precursor synthesis by SbnI, SbnA and SbnB in the NCTC 8325 reference. SbnI forms phosphoserine; SbnA forms ACEGA with glutamate; SbnB forms L-Dap and 2-oxoglutarate. No direct enzyme-enzyme interaction or regulation is asserted. Ionic chemical participants follow UniProt cross-references and cached ChEBI labels. ATP/redox/co-products are described in evidence; the graph is not a complete stoichiometric model. No native flux or experimental-stock identity.

SubjectPredicateObjectNotesEvidence
L-serine zwitterion is a substrate for SbnI (SAOUHSC_00083; NCTC 8325 reference) ATP-dependent phosphorylation of free L-serine to O-phospho-L-serine, releasing ADP and a proton.
https://www.uniprot.org/uniprotkb/Q2G1M5
https://www.ncbi.nlm.nih.gov/protein/SQF72453.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M5
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 254 aa; sbnI, SAOUHSC_00083; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent phosphorylation of free L-serine to O-phospho-L-serine, releasing ADP and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:29483190; RHEA:59112 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1074/jbc.ra118.001875 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation. No heme sensing, DNA binding, regulation or PDB construct identity is adopted.
    snippet
    Free serine kinase that uses ATP to phosphorylate L-serine to yield O-phospho-L-serine and ADP.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72453.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 254-aa SQF72453.1 sequence equals Q2G1M5. CDS LS483365.1:89680..90444, locus NCTC8325_00073, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
SbnI (SAOUHSC_00083; NCTC 8325 reference) forms O-phosphonato-L-serine(2-) ATP-dependent phosphorylation of free L-serine to O-phospho-L-serine, releasing ADP and a proton.
https://www.uniprot.org/uniprotkb/Q2G1M5
https://www.ncbi.nlm.nih.gov/protein/SQF72453.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M5
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 254 aa; sbnI, SAOUHSC_00083; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent phosphorylation of free L-serine to O-phospho-L-serine, releasing ADP and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:29483190; RHEA:59112 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1074/jbc.ra118.001875 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation. No heme sensing, DNA binding, regulation or PDB construct identity is adopted.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72453.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 254-aa SQF72453.1 sequence equals Q2G1M5. CDS LS483365.1:89680..90444, locus NCTC8325_00073, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
O-phosphonato-L-serine(2-) is a substrate for SbnA (SAOUHSC_00075; NCTC 8325 reference) O-phospho-L-serine and L-glutamate form ACEGA, phosphate and a proton.
https://www.uniprot.org/uniprotkb/Q2G1N3
https://www.ncbi.nlm.nih.gov/protein/SQF72445.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 109, sequence version 2; 326 aa; sbnA, SAOUHSC_00075; S. aureus NCTC 8325 / PS 47, taxon 93061. O-phospho-L-serine and L-glutamate form ACEGA, phosphate and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:24485762; RHEA:52384 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1016/j.chembiol.2013.12.011 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
    snippet
    Catalyzes the synthesis of N-((2S)-2-amino-2-carboxyethyl)-L-glutamate (ACEGA) from O-phospho-L-serine and L-glutamate.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72445.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 326-aa SQF72445.1 sequence equals Q2G1N3. CDS LS483365.1:79227..80207, locus NCTC8325_00065, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Older ABD29258.1 is only 281 aa and is marked truncated by UniProt; it is not the adopted model. AAP82063.1 also matches 326 aa but its deposit has species taxon 1280 and no strain qualifier. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
L-glutamate(1-) is a substrate for SbnA (SAOUHSC_00075; NCTC 8325 reference) O-phospho-L-serine and L-glutamate form ACEGA, phosphate and a proton.
https://www.uniprot.org/uniprotkb/Q2G1N3
https://www.ncbi.nlm.nih.gov/protein/SQF72445.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 109, sequence version 2; 326 aa; sbnA, SAOUHSC_00075; S. aureus NCTC 8325 / PS 47, taxon 93061. O-phospho-L-serine and L-glutamate form ACEGA, phosphate and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:24485762; RHEA:52384 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1016/j.chembiol.2013.12.011 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72445.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 326-aa SQF72445.1 sequence equals Q2G1N3. CDS LS483365.1:79227..80207, locus NCTC8325_00065, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Older ABD29258.1 is only 281 aa and is marked truncated by UniProt; it is not the adopted model. AAP82063.1 also matches 326 aa but its deposit has species taxon 1280 and no strain qualifier. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
SbnA (SAOUHSC_00075; NCTC 8325 reference) forms N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate(2-) O-phospho-L-serine and L-glutamate form ACEGA, phosphate and a proton.
https://www.uniprot.org/uniprotkb/Q2G1N3
https://www.ncbi.nlm.nih.gov/protein/SQF72445.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N3
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 109, sequence version 2; 326 aa; sbnA, SAOUHSC_00075; S. aureus NCTC 8325 / PS 47, taxon 93061. O-phospho-L-serine and L-glutamate form ACEGA, phosphate and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:24485762; RHEA:52384 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1016/j.chembiol.2013.12.011 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72445.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 326-aa SQF72445.1 sequence equals Q2G1N3. CDS LS483365.1:79227..80207, locus NCTC8325_00065, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Older ABD29258.1 is only 281 aa and is marked truncated by UniProt; it is not the adopted model. AAP82063.1 also matches 326 aa but its deposit has species taxon 1280 and no strain qualifier. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate(2-) is a substrate for SbnB (SAOUHSC_00076; NCTC 8325 reference) NAD(+)-dependent oxidative hydrolysis of ACEGA with water forms L-Dap and 2-oxoglutarate, NADH and a proton.
https://www.uniprot.org/uniprotkb/Q2G1N2
https://www.ncbi.nlm.nih.gov/protein/SQF72446.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N2
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 110, sequence version 1; 336 aa; sbnB, SAOUHSC_00076; S. aureus NCTC 8325 / PS 47, taxon 93061. NAD(+)-dependent oxidative hydrolysis of ACEGA with water forms L-Dap and 2-oxoglutarate, NADH and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:24485762; RHEA:51928 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1016/j.chembiol.2013.12.011 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
    snippet
    Catalyzes the hydrolysis of N-((2S)-2-amino-2-carboxyethyl)-L-glutamate (ACEGA) to form L-2,3-diaminopropionic acid and 2-oxoglutarate.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72446.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 336-aa SQF72446.1 sequence equals Q2G1N2. CDS LS483365.1:80204..81214, locus NCTC8325_00066, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
SbnB (SAOUHSC_00076; NCTC 8325 reference) forms 3-amino-L-alanine zwitterion NAD(+)-dependent oxidative hydrolysis of ACEGA with water forms L-Dap and 2-oxoglutarate, NADH and a proton.
https://www.uniprot.org/uniprotkb/Q2G1N2
https://www.ncbi.nlm.nih.gov/protein/SQF72446.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N2
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 110, sequence version 1; 336 aa; sbnB, SAOUHSC_00076; S. aureus NCTC 8325 / PS 47, taxon 93061. NAD(+)-dependent oxidative hydrolysis of ACEGA with water forms L-Dap and 2-oxoglutarate, NADH and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:24485762; RHEA:51928 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1016/j.chembiol.2013.12.011 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72446.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 336-aa SQF72446.1 sequence equals Q2G1N2. CDS LS483365.1:80204..81214, locus NCTC8325_00066, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
SbnB (SAOUHSC_00076; NCTC 8325 reference) forms 2-oxoglutarate(2-) NAD(+)-dependent oxidative hydrolysis of ACEGA with water forms L-Dap and 2-oxoglutarate, NADH and a proton.
https://www.uniprot.org/uniprotkb/Q2G1N2
https://www.ncbi.nlm.nih.gov/protein/SQF72446.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N2
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 110, sequence version 1; 336 aa; sbnB, SAOUHSC_00076; S. aureus NCTC 8325 / PS 47, taxon 93061. NAD(+)-dependent oxidative hydrolysis of ACEGA with water forms L-Dap and 2-oxoglutarate, NADH and a proton. FUNCTION and CATALYTIC ACTIVITY cite PMID:24485762; RHEA:51928 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1016/j.chembiol.2013.12.011 was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72446.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 336-aa SQF72446.1 sequence equals Q2G1N2. CDS LS483365.1:80204..81214, locus NCTC8325_00066, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.

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

Causal graph — biosynthesis 8 nodes, 8 edges

Database-qualified assembly steps 1-3: SbnE condensation, SbnH decarboxylation and SbnF condensation. The product CHEBI:142971 is the acceptor in the separately retained terminal SbnC graph; all node references here remain graph-local. SbnE/SbnH match LS483365 proteins; SbnF denotes the 616-aa CP000253 reference, not the shorter 592-aa LS483365 model. No sequence or stock equivalence is asserted between those SbnF models. New functional claims are database assertions, not independently re-read primary experiments. Original SbnC graph and evidence remain unchanged.

SubjectPredicateObjectNotesEvidence
3-amino-L-alanine zwitterion is a substrate for SbnE (SAOUHSC_00079; NCTC 8325 reference) ATP-dependent condensation of L-Dap and citrate forms citryl-L-Dap, AMP and diphosphate; assembly step 1.
https://www.uniprot.org/uniprotkb/Q2G1M9
https://www.ncbi.nlm.nih.gov/protein/SQF72449.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M9
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 578 aa; sbnE, SAOUHSC_00079; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent condensation of L-Dap and citrate forms citryl-L-Dap, AMP and diphosphate; assembly step 1. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59124 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
    snippet
    the first step in staphyloferrin B biosynthesis
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72449.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 578-aa SQF72449.1 sequence equals Q2G1M9. CDS LS483365.1:84228..85964, locus NCTC8325_00069, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
citrate(3-) is a substrate for SbnE (SAOUHSC_00079; NCTC 8325 reference) ATP-dependent condensation of L-Dap and citrate forms citryl-L-Dap, AMP and diphosphate; assembly step 1.
https://www.uniprot.org/uniprotkb/Q2G1M9
https://www.ncbi.nlm.nih.gov/protein/SQF72449.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M9
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 578 aa; sbnE, SAOUHSC_00079; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent condensation of L-Dap and citrate forms citryl-L-Dap, AMP and diphosphate; assembly step 1. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59124 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72449.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 578-aa SQF72449.1 sequence equals Q2G1M9. CDS LS483365.1:84228..85964, locus NCTC8325_00069, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
SbnE (SAOUHSC_00079; NCTC 8325 reference) forms 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate(2-) ATP-dependent condensation of L-Dap and citrate forms citryl-L-Dap, AMP and diphosphate; assembly step 1.
https://www.uniprot.org/uniprotkb/Q2G1M9
https://www.ncbi.nlm.nih.gov/protein/SQF72449.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M9
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 578 aa; sbnE, SAOUHSC_00079; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent condensation of L-Dap and citrate forms citryl-L-Dap, AMP and diphosphate; assembly step 1. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59124 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72449.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 578-aa SQF72449.1 sequence equals Q2G1M9. CDS LS483365.1:84228..85964, locus NCTC8325_00069, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate(2-) is a substrate for SbnH (SAOUHSC_00082; NCTC 8325 reference) Decarboxylation of citryl-L-Dap with a proton forms citryl-diaminoethane and carbon dioxide; assembly step 2.
https://www.uniprot.org/uniprotkb/Q2G1M6
https://www.ncbi.nlm.nih.gov/protein/SQF72452.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M6
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 112, sequence version 1; 400 aa; sbnH, SAOUHSC_00082; S. aureus NCTC 8325 / PS 47, taxon 93061. Decarboxylation of citryl-L-Dap with a proton forms citryl-diaminoethane and carbon dioxide; assembly step 2. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59120 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
    snippet
    Catalyzes the decarboxylation of citryl-L-2,3-diaminopropionic acid to citryl-diaminoethane
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72452.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 400-aa SQF72452.1 sequence equals Q2G1M6. CDS LS483365.1:88474..89676, locus NCTC8325_00072, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
SbnH (SAOUHSC_00082; NCTC 8325 reference) forms 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate Decarboxylation of citryl-L-Dap with a proton forms citryl-diaminoethane and carbon dioxide; assembly step 2.
https://www.uniprot.org/uniprotkb/Q2G1M6
https://www.ncbi.nlm.nih.gov/protein/SQF72452.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M6
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 112, sequence version 1; 400 aa; sbnH, SAOUHSC_00082; S. aureus NCTC 8325 / PS 47, taxon 93061. Decarboxylation of citryl-L-Dap with a proton forms citryl-diaminoethane and carbon dioxide; assembly step 2. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59120 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/SQF72452.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 400-aa SQF72452.1 sequence equals Q2G1M6. CDS LS483365.1:88474..89676, locus NCTC8325_00072, independently translates to it using table 11 and codon_start 1. LS483365 names NCTC8325, taxon 93061, BioSample SAMEA3672889. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate is a substrate for SbnF (SAOUHSC_00080; NCTC 8325 reference) ATP-dependent condensation of citryl-diaminoethane and L-Dap forms the SbnC acceptor, AMP and diphosphate; assembly step 3.
https://www.uniprot.org/uniprotkb/Q2G1M8
https://www.ncbi.nlm.nih.gov/protein/ABD29263.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 616 aa; sbnF, SAOUHSC_00080; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent condensation of citryl-diaminoethane and L-Dap forms the SbnC acceptor, AMP and diphosphate; assembly step 3. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59128 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
    snippet
    the third step in staphyloferrin B biosynthesis
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ABD29263.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 616-aa ABD29263.1 sequence equals canonical Q2G1M8; CDS CP000253.1:86396..88246, SAOUHSC_00080, independently translates to it using table 11 and codon_start 1. CP000253 names NCTC 8325, taxon 93061, BioSample SAMN02604235. The owner-linked LS483365 model SQF72450.1 (LS483365.1:85945..87723; NCTC8325_00070) is 592 aa, not the canonical sequence; it comes from a different BioSample, SAMEA3672889. No functional assignment to this shorter model or equivalence of the two stocks is asserted. LS483365 labels that shorter CDS iucC_1. AAP82068.1 is a separate 579-aa species-level deposit, flagged by UniProt for truncated initiation, not the adopted 616-aa model. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
3-amino-L-alanine zwitterion is a substrate for SbnF (SAOUHSC_00080; NCTC 8325 reference) ATP-dependent condensation of citryl-diaminoethane and L-Dap forms the SbnC acceptor, AMP and diphosphate; assembly step 3.
https://www.uniprot.org/uniprotkb/Q2G1M8
https://www.ncbi.nlm.nih.gov/protein/ABD29263.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 616 aa; sbnF, SAOUHSC_00080; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent condensation of citryl-diaminoethane and L-Dap forms the SbnC acceptor, AMP and diphosphate; assembly step 3. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59128 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ABD29263.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 616-aa ABD29263.1 sequence equals canonical Q2G1M8; CDS CP000253.1:86396..88246, SAOUHSC_00080, independently translates to it using table 11 and codon_start 1. CP000253 names NCTC 8325, taxon 93061, BioSample SAMN02604235. The owner-linked LS483365 model SQF72450.1 (LS483365.1:85945..87723; NCTC8325_00070) is 592 aa, not the canonical sequence; it comes from a different BioSample, SAMEA3672889. No functional assignment to this shorter model or equivalence of the two stocks is asserted. LS483365 labels that shorter CDS iucC_1. AAP82068.1 is a separate 579-aa species-level deposit, flagged by UniProt for truncated initiation, not the adopted 616-aa model. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.
SbnF (SAOUHSC_00080; NCTC 8325 reference) forms 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate ATP-dependent condensation of citryl-diaminoethane and L-Dap forms the SbnC acceptor, AMP and diphosphate; assembly step 3.
https://www.uniprot.org/uniprotkb/Q2G1M8
https://www.ncbi.nlm.nih.gov/protein/ABD29263.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1M8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 101, sequence version 1; 616 aa; sbnF, SAOUHSC_00080; S. aureus NCTC 8325 / PS 47, taxon 93061. ATP-dependent condensation of citryl-diaminoethane and L-Dap forms the SbnC acceptor, AMP and diphosphate; assembly step 3. FUNCTION and CATALYTIC ACTIVITY cite PMID:19775248; RHEA:59128 and its forward direction are read from UniProt, not independently verified against Rhea. DOI:10.1111/j.1365-2958.2009.06880.x was tool-inaccessible; no new PRIMARY_EXPERIMENT claim. Chemical identifiers are the ionic participants cross-referenced by UniProt; labels checked against cached ChEBI release 255. Graph edges summarize principal substrates/products, not a complete stoichiometric equation.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ABD29263.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 616-aa ABD29263.1 sequence equals canonical Q2G1M8; CDS CP000253.1:86396..88246, SAOUHSC_00080, independently translates to it using table 11 and codon_start 1. CP000253 names NCTC 8325, taxon 93061, BioSample SAMN02604235. The owner-linked LS483365 model SQF72450.1 (LS483365.1:85945..87723; NCTC8325_00070) is 592 aa, not the canonical sequence; it comes from a different BioSample, SAMEA3672889. No functional assignment to this shorter model or equivalence of the two stocks is asserted. LS483365 labels that shorter CDS iucC_1. AAP82068.1 is a separate 579-aa species-level deposit, flagged by UniProt for truncated initiation, not the adopted 616-aa model. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.

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

Causal graph — biosynthesis 2 nodes, 1 edge

Database-qualified involvement of canonical SbnD in staphyloferrin B secretion. This is the 418-aa CP000253 reference, not the 390-aa LS483365 protein; neither exclusive transport nor essentiality is asserted. The compound node denotes the neutral owner, not a verified transported charge state.

SubjectPredicateObjectNotesEvidence
SbnD (SAOUHSC_00078; NCTC 8325 reference) is involved in secretion of staphyloferrin B Partial impairment in the database disruption annotation does not establish loss of secretion. The neutral parent is used as the compound anchor only; transported protonation state and direct substrate specificity are unresolved.
https://www.uniprot.org/uniprotkb/Q2G1N0
https://www.ncbi.nlm.nih.gov/protein/ABD29261.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2G1N0
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed UniProt entry version 117, sequence version 1; 418 aa; sbnD, SAOUHSC_00078; S. aureus NCTC 8325 / PS 47, taxon 93061. FUNCTION cites ECO:0000269/PMID:25680529 for involvement in staphyloferrin B secretion. The disruption annotation reports partial impairment, not abolished secretion or essentiality. DOI:10.1016/j.febslet.2015.02.002 was not independently inspected. No direct transport assay, rate, specificity, topology or transported ionic species is asserted.
    snippet
    Involved in staphyloferrin B secretion
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ABD29261.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 418-aa ABD29261.1 sequence equals canonical Q2G1N0; CDS CP000253.1:83505..84761, SAOUHSC_00078, independently translates to it using table 11 and codon_start 1. CP000253 names NCTC 8325, taxon 93061, BioSample SAMN02604235. The owner-linked LS483365 model SQF72448.1 (LS483365.1:83066..84238; NCTC8325_00068) is 390 aa, not the canonical sequence; it comes from a different BioSample, SAMEA3672889. No functional assignment to this shorter model or equivalence of the two stocks is asserted. Sequence equality grounds a reference only, not an assayed construct, historical stock, native expression or function. Source/genomic annotations are not functional experiments.

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

Causal graph — biosynthesis 5 nodes, 4 edges

Bounded genetic evidence for Newman SbnA and SbnB, with deliberately selected canonical references. Newman-derived delta-sfa background, not the owner's NCTC 8325 BGC stock. Insertional inactivation, not a clean deletion or an independently sequenced mutant. The paper reports absence of staphyloferrin B in mutant spent supernatants by ESI-MS in iron-limited medium without added transferrin; those spectra are data not shown. Growth and CAS readouts are not compound-specific concentration measurements. The neutral owner is the author-assigned compound anchor, not an independently verified protonation state, absolute stereopurity or ferric-complex assignment. No direct catalysis, physical SbnA-SbnB complex, exclusive pathway, producer/BGC, virulence or origin upgrade.

SubjectPredicateObjectNotesEvidence
H2131: sbnA insertion in Newman delta-sfa background disrupts_gene_represented_by SbnA (NWMN_0060; Newman reference) The canonical protein represents the named gene, not the altered allele. Canonical 326-aa A6QDA0 matches all residues of BAF66332.1 and the independently translated complete CDS AP009351.1:79725..80705, table 11, codon_start 1, TTG start and TGA stop. Native source taxon 426430, strain Newman, BioSample SAMD00060913. Sequence also equals the previously inspected NCTC 8325 reference Q2G1N3; this is a distinct strain-specific accession, not a new amino-acid sequence. Reference equality does not verify historical experimental stock, insertion allele, complete plasmid, expression, processing or function.
DOI:10.1186/1471-2180-11-199
https://www.uniprot.org/uniprotkb/A6QDA0
https://www.ncbi.nlm.nih.gov/nuccore/AP009351.1
  • reference
    DOI:10.1186/1471-2180-11-199
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table 1 identifies H2131 and the sbnA insertion; Methods and Results specify the Newman delta-sfa genetic background. Newman-derived delta-sfa background, not the owner's NCTC 8325 BGC stock. Insertional inactivation, not a clean deletion or an independently sequenced mutant. The paper reports absence of staphyloferrin B in mutant spent supernatants by ESI-MS in iron-limited medium without added transferrin; those spectra are data not shown. Growth and CAS readouts are not compound-specific concentration measurements. The neutral owner is the author-assigned compound anchor, not an independently verified protonation state, absolute stereopurity or ferric-complex assignment. No direct catalysis, physical SbnA-SbnB complex, exclusive pathway, producer/BGC, virulence or origin upgrade.
  • reference
    https://www.uniprot.org/uniprotkb/A6QDA0
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-10
    notes
    UniProt release 2026_03, entry 95, sequence 1. Reviewed; gene sbnA/NWMN_0060 and reference PMID:21906287 directly link the Newman entry to the inspected 2011 study. Its exact catalytic reaction cites later work, not a demonstrated reaction in this 2011 paper.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP009351.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-10
    notes
    Canonical 326-aa A6QDA0 matches all residues of BAF66332.1 and the independently translated complete CDS AP009351.1:79725..80705, table 11, codon_start 1, TTG start and TGA stop. Native source taxon 426430, strain Newman, BioSample SAMD00060913. Sequence also equals the previously inspected NCTC 8325 reference Q2G1N3; this is a distinct strain-specific accession, not a new amino-acid sequence. Reference equality does not verify historical experimental stock, insertion allele, complete plasmid, expression, processing or function.
H2131: sbnA insertion in Newman delta-sfa background has_reported_loss_of staphyloferrin B Reported loss in the stated genetic and culture context, not a universal essentiality or zero-concentration measurement. Newman-derived delta-sfa background, not the owner's NCTC 8325 BGC stock. Insertional inactivation, not a clean deletion or an independently sequenced mutant. The paper reports absence of staphyloferrin B in mutant spent supernatants by ESI-MS in iron-limited medium without added transferrin; those spectra are data not shown. Growth and CAS readouts are not compound-specific concentration measurements. The neutral owner is the author-assigned compound anchor, not an independently verified protonation state, absolute stereopurity or ferric-complex assignment. No direct catalysis, physical SbnA-SbnB complex, exclusive pathway, producer/BGC, virulence or origin upgrade.
DOI:10.1186/1471-2180-11-199
  • reference
    DOI:10.1186/1471-2180-11-199
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Results report the compound in parental delta-sfa supernatant and its absence in the insertion mutants; ESI-MS data not shown. Figures 1-2 show growth/CAS corroboration and complementation, not raw compound spectra. Newman-derived delta-sfa background, not the owner's NCTC 8325 BGC stock. Insertional inactivation, not a clean deletion or an independently sequenced mutant. The paper reports absence of staphyloferrin B in mutant spent supernatants by ESI-MS in iron-limited medium without added transferrin; those spectra are data not shown. Growth and CAS readouts are not compound-specific concentration measurements. The neutral owner is the author-assigned compound anchor, not an independently verified protonation state, absolute stereopurity or ferric-complex assignment. No direct catalysis, physical SbnA-SbnB complex, exclusive pathway, producer/BGC, virulence or origin upgrade.
    snippet
    absent in the spent culture supernatants
H1718: sbnB insertion in Newman delta-sfa background disrupts_gene_represented_by SbnB (NWMN_0061; Newman reference) The canonical protein represents the named gene, not the altered allele. Canonical 336-aa A0A0H3K9Y6 matches all residues of BAF66333.1 and the independently translated complete CDS AP009351.1:80702..81712, table 11, codon_start 1, ATG start and TAA stop. Native source taxon 426430, strain Newman, BioSample SAMD00060913. Sequence also equals the previously inspected NCTC 8325 reference Q2G1N2; this is a distinct strain-specific accession, not a new amino-acid sequence. Reference equality does not verify historical experimental stock, insertion allele, complete plasmid, expression, processing or function.
DOI:10.1186/1471-2180-11-199
https://www.uniprot.org/uniprotkb/A0A0H3K9Y6
https://www.ncbi.nlm.nih.gov/nuccore/AP009351.1
  • reference
    DOI:10.1186/1471-2180-11-199
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Table 1 identifies H1718 and the sbnB insertion; Methods and Results specify the Newman delta-sfa genetic background. Newman-derived delta-sfa background, not the owner's NCTC 8325 BGC stock. Insertional inactivation, not a clean deletion or an independently sequenced mutant. The paper reports absence of staphyloferrin B in mutant spent supernatants by ESI-MS in iron-limited medium without added transferrin; those spectra are data not shown. Growth and CAS readouts are not compound-specific concentration measurements. The neutral owner is the author-assigned compound anchor, not an independently verified protonation state, absolute stereopurity or ferric-complex assignment. No direct catalysis, physical SbnA-SbnB complex, exclusive pathway, producer/BGC, virulence or origin upgrade.
  • reference
    https://www.uniprot.org/uniprotkb/A0A0H3K9Y6
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-10
    notes
    UniProt release 2026_03, entry 53, sequence 1. Unreviewed; gene sbnB/NWMN_0061 and native BAF66333.1 establish the selected reference. The inherited ornithine-cyclodeaminase label is not adopted as function; no FUNCTION or CATALYTIC ACTIVITY comment is present. PDB-derived binding annotations and a PROSITE propagation caution do not establish the 2011 construct or mechanism.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP009351.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-10
    notes
    Canonical 336-aa A0A0H3K9Y6 matches all residues of BAF66333.1 and the independently translated complete CDS AP009351.1:80702..81712, table 11, codon_start 1, ATG start and TAA stop. Native source taxon 426430, strain Newman, BioSample SAMD00060913. Sequence also equals the previously inspected NCTC 8325 reference Q2G1N2; this is a distinct strain-specific accession, not a new amino-acid sequence. Reference equality does not verify historical experimental stock, insertion allele, complete plasmid, expression, processing or function.
H1718: sbnB insertion in Newman delta-sfa background has_reported_loss_of staphyloferrin B Reported loss in the stated genetic and culture context, not a universal essentiality or zero-concentration measurement. Newman-derived delta-sfa background, not the owner's NCTC 8325 BGC stock. Insertional inactivation, not a clean deletion or an independently sequenced mutant. The paper reports absence of staphyloferrin B in mutant spent supernatants by ESI-MS in iron-limited medium without added transferrin; those spectra are data not shown. Growth and CAS readouts are not compound-specific concentration measurements. The neutral owner is the author-assigned compound anchor, not an independently verified protonation state, absolute stereopurity or ferric-complex assignment. No direct catalysis, physical SbnA-SbnB complex, exclusive pathway, producer/BGC, virulence or origin upgrade.
DOI:10.1186/1471-2180-11-199
  • reference
    DOI:10.1186/1471-2180-11-199
    evidence type
    PRIMARY_EXPERIMENT
    notes
    Results report the compound in parental delta-sfa supernatant and its absence in the insertion mutants; ESI-MS data not shown. Figures 1-2 show growth/CAS corroboration and complementation, not raw compound spectra. Newman-derived delta-sfa background, not the owner's NCTC 8325 BGC stock. Insertional inactivation, not a clean deletion or an independently sequenced mutant. The paper reports absence of staphyloferrin B in mutant spent supernatants by ESI-MS in iron-limited medium without added transferrin; those spectra are data not shown. Growth and CAS readouts are not compound-specific concentration measurements. The neutral owner is the author-assigned compound anchor, not an independently verified protonation state, absolute stereopurity or ferric-complex assignment. No direct catalysis, physical SbnA-SbnB complex, exclusive pathway, producer/BGC, virulence or origin upgrade.

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

Explore across X-Mech

AntibioticMech (staphyloferrin B) ↗ MediaIngredientMech (CHEBI:134612) ↗ TaxonMech: Staphylococcus aureus subsp. aureus NCTC 8325 (NCBITaxon:93061) ↗ PathwayMech (mibig:BGC0000943) ↗

Provenance

Source conceptSourceVersion
BGC0000943MIBIG5
CHEBI:134612CHEBI3-star

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