staphyloferrin A biosynthesis

MetaCyc:PWY-7990

Complete three-transformation staphyloferrin A biosynthesis scoped to Staphylococcus aureus Newman: L-ornithine racemization supplies D-ornithine, followed by the ordered SfaD and SfaB citrate ligations. The selected racemization direction is pathway flux; native MetaCyc and KEGG describe the reversible reaction. SfaC/NWMN_2079 activity remains inferred from locus function, sequence-family evidence and the native assignment, not an isolated Newman enzyme assay. Its PLP relation is an automatic annotation transferred through exact sequence equality, not a direct binding measurement. Newman SfaB and SfaD coding regions were used in the inspected 2010 recombinant preparation; full engineered construct sequences and native assembly states are unresolved. The 2009 Cotton evidence for ordered individual ligations was inspected as an abstract only. Current NCTC 8325 annotations inform reaction identity: SfaB is sequence-identical to the selected Newman protein, whereas SfaD differs at residue 532 and is not treated as the same protein. The native ligase Mg2+ assertions are retained as qualified curated cofactor assignments rather than a unique physiological metal or binding stoichiometry. Current Rhea/ChEBI chemistry specifies the N5-(S)-citryl intermediate and N2-(R),N5-(S)-citryl product, whereas native CPD-21047 and CPD-12589 leave the citryl centers unspecified. The inspected 2010 ferric receptor-bound structure supports final N2 R/N5 S stereochemistry; it does not directly establish the free intermediate's stereochemistry or the selected free ionic forms. These forms remain explicit current chemical-authority conventions, without exact native-compound equivalence. Iron/Fur-dependent transcription is reported as context; transport, ferric loading, uptake, citrate production and the distinct staphyloferrin B route lie outside this complete biosynthetic boundary.

Pathway type

staphyloferrin a biosynthesis

Organism scope

Staphylococcus aureus subsp. aureus str. Newman NCBITaxon:426430

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Pathway network

19 nodes · 31 asserted directed edges

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Reaction / activity
Chemical / cofactor
Protein / complex
Taxon
Pathway
Solid arrow: mechanistic relation
Dashed arrow: membership, location or cofactor relation

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Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Staphylococcus aureus subsp. aureus str. Newman `NCBITaxon:426430`	taxon
N(5)-[(S)-citryl]-D-ornithine(2-) `CHEBI:142972`	small molecule
staphyloferrin A(5-) `CHEBI:142973`	small molecule
hydron `CHEBI:15378`	small molecule
citrate(3-) `CHEBI:16947`	small molecule
magnesium(2+) `CHEBI:18420`	cofactor
ATP(4-) `CHEBI:30616`	small molecule
diphosphate(3-) `CHEBI:33019`	small molecule
adenosine 5'-monophosphate(2-) `CHEBI:456215`	small molecule
L-ornithinium(1+) `CHEBI:46911`	small molecule
D-ornithinium(1+) `CHEBI:57668`	small molecule
pyridoxal 5'-phosphate(2-) `CHEBI:597326`	cofactor
NWMN_2079 `NCBIProtein:BAF68351.1`	protein
NWMN_2080 `NCBIProtein:BAF68352.1`	protein
NWMN_2082 `NCBIProtein:BAF68354.1`	protein
L-Ornithine racemization toward D-ornithine `RHEA:11585`	molecular activity	left to right
SfaD D-ornithine N5-citrylation `RHEA:59137`	molecular activity	left to right
SfaB terminal N2-citrylation `RHEA:59141`	molecular activity	left to right

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
L-ornithinium(1+) `CHEBI:46911`	consumes	L-Ornithine racemization toward D-ornithine `RHEA:11585`	RHEA:11585 Source assertion: The selected Rhea direction assigns CHEBI:46911 to its substrates with coefficient 1. Source location `rh:11585/rh:substrates -> http://rdf.rhea-db.org/11584_L; rh:contains1 -> http://rdf.rhea-db.org/Participant_11584_compound_1826; rh:compound -> http://rdf.rhea-db.org/Compound_1826; rh:chebi`
L-Ornithine racemization toward D-ornithine `RHEA:11585`	produces	D-ornithinium(1+) `CHEBI:57668`	RHEA:11585 Source assertion: The selected Rhea direction assigns CHEBI:57668 to its products with coefficient 1. Source location `rh:11585/rh:products -> http://rdf.rhea-db.org/11584_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_11584_compound_5090; rh:compound -> http://rdf.rhea-db.org/Compound_5090; rh:chebi`
D-ornithinium(1+) `CHEBI:57668`	consumes	SfaD D-ornithine N5-citrylation `RHEA:59137`	RHEA:59137 Source assertion: The selected Rhea direction assigns CHEBI:57668 to its substrates with coefficient 1. Source location `rh:59137/rh:substrates -> http://rdf.rhea-db.org/59136_L; rh:contains1 -> http://rdf.rhea-db.org/Participant_59136_compound_5090; rh:compound -> http://rdf.rhea-db.org/Compound_5090; rh:chebi`
citrate(3-) `CHEBI:16947`	consumes	SfaD D-ornithine N5-citrylation `RHEA:59137`	RHEA:59137 Source assertion: The selected Rhea direction assigns CHEBI:16947 to its substrates with coefficient 1. Source location `rh:59137/rh:substrates -> http://rdf.rhea-db.org/59136_L; rh:contains1 -> http://rdf.rhea-db.org/Participant_59136_compound_5244; rh:compound -> http://rdf.rhea-db.org/Compound_5244; rh:chebi`
ATP(4-) `CHEBI:30616`	consumes	SfaD D-ornithine N5-citrylation `RHEA:59137`	RHEA:59137 Source assertion: The selected Rhea direction assigns CHEBI:30616 to its substrates with coefficient 1. Source location `rh:59137/rh:substrates -> http://rdf.rhea-db.org/59136_L; rh:contains1 -> http://rdf.rhea-db.org/Participant_59136_compound_6372; rh:compound -> http://rdf.rhea-db.org/Compound_6372; rh:chebi`
SfaD D-ornithine N5-citrylation `RHEA:59137`	produces This edge uses the current Rhea/ChEBI stereospecific free ionic form. The corresponding native MetaCyc compound leaves citryl stereochemistry unspecified; no exact equivalence is asserted.	N(5)-[(S)-citryl]-D-ornithine(2-) `CHEBI:142972`	RHEA:59137 Source assertion: The selected Rhea direction assigns CHEBI:142972 to its products with coefficient 1. Source location `rh:59137/rh:products -> http://rdf.rhea-db.org/59136_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59136_compound_15298; rh:compound -> http://rdf.rhea-db.org/Compound_15298; rh:chebi` CHEBI:142973 Source assertion: CHEBI:142972 defines N(5)-[(S)-citryl]-D-ornithine(2-) with its specified stereochemistry and charge -2. This is the current free chemical identity, distinct from the broader native compound. Source location `statements[subject="CHEBI:142972",predicate=rdfs:label\|chemrof:inchi_string\|chemrof:charge]`
SfaD D-ornithine N5-citrylation `RHEA:59137`	produces	adenosine 5'-monophosphate(2-) `CHEBI:456215`	RHEA:59137 Source assertion: The selected Rhea direction assigns CHEBI:456215 to its products with coefficient 1. Source location `rh:59137/rh:products -> http://rdf.rhea-db.org/59136_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59136_compound_2590; rh:compound -> http://rdf.rhea-db.org/Compound_2590; rh:chebi`
SfaD D-ornithine N5-citrylation `RHEA:59137`	produces	diphosphate(3-) `CHEBI:33019`	RHEA:59137 Source assertion: The selected Rhea direction assigns CHEBI:33019 to its products with coefficient 1. Source location `rh:59137/rh:products -> http://rdf.rhea-db.org/59136_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59136_compound_2106; rh:compound -> http://rdf.rhea-db.org/Compound_2106; rh:chebi`
SfaD D-ornithine N5-citrylation `RHEA:59137`	produces	hydron `CHEBI:15378`	RHEA:59137 Source assertion: The selected Rhea direction assigns CHEBI:15378 to its products with coefficient 1. Source location `rh:59137/rh:products -> http://rdf.rhea-db.org/59136_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59136_compound_3249; rh:compound -> http://rdf.rhea-db.org/Compound_3249; rh:chebi`
N(5)-[(S)-citryl]-D-ornithine(2-) `CHEBI:142972`	consumes This edge uses the current Rhea/ChEBI stereospecific free ionic form. The corresponding native MetaCyc compound leaves citryl stereochemistry unspecified; no exact equivalence is asserted.	SfaB terminal N2-citrylation `RHEA:59141`	RHEA:59141 Source assertion: The selected Rhea direction assigns CHEBI:142972 to its substrates with coefficient 1. Source location `rh:59141/rh:substrates -> http://rdf.rhea-db.org/59140_L; rh:contains1 -> http://rdf.rhea-db.org/Participant_59140_compound_15298; rh:compound -> http://rdf.rhea-db.org/Compound_15298; rh:chebi` CHEBI:142973 Source assertion: CHEBI:142972 defines N(5)-[(S)-citryl]-D-ornithine(2-) with its specified stereochemistry and charge -2. This is the current free chemical identity, distinct from the broader native compound. Source location `statements[subject="CHEBI:142972",predicate=rdfs:label\|chemrof:inchi_string\|chemrof:charge]`
citrate(3-) `CHEBI:16947`	consumes	SfaB terminal N2-citrylation `RHEA:59141`	RHEA:59141 Source assertion: The selected Rhea direction assigns CHEBI:16947 to its substrates with coefficient 1. Source location `rh:59141/rh:substrates -> http://rdf.rhea-db.org/59140_L; rh:contains1 -> http://rdf.rhea-db.org/Participant_59140_compound_5244; rh:compound -> http://rdf.rhea-db.org/Compound_5244; rh:chebi`
ATP(4-) `CHEBI:30616`	consumes	SfaB terminal N2-citrylation `RHEA:59141`	RHEA:59141 Source assertion: The selected Rhea direction assigns CHEBI:30616 to its substrates with coefficient 1. Source location `rh:59141/rh:substrates -> http://rdf.rhea-db.org/59140_L; rh:contains1 -> http://rdf.rhea-db.org/Participant_59140_compound_6372; rh:compound -> http://rdf.rhea-db.org/Compound_6372; rh:chebi`
SfaB terminal N2-citrylation `RHEA:59141`	produces This edge uses the current Rhea/ChEBI stereospecific free ionic form. The corresponding native MetaCyc compound leaves citryl stereochemistry unspecified; no exact equivalence is asserted.	staphyloferrin A(5-) `CHEBI:142973`	RHEA:59141 Source assertion: The selected Rhea direction assigns CHEBI:142973 to its products with coefficient 1. Source location `rh:59141/rh:products -> http://rdf.rhea-db.org/59140_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59140_compound_15299; rh:compound -> http://rdf.rhea-db.org/Compound_15299; rh:chebi` CHEBI:142973 Source assertion: CHEBI:142973 defines staphyloferrin A(5-) with its specified stereochemistry and charge -5. This is the current free chemical identity, distinct from the broader native compound. Source location `statements[subject="CHEBI:142973",predicate=rdfs:label\|chemrof:inchi_string\|chemrof:charge]` PMID:20147287 Source assertion: The ferric receptor-bound product model assigns ornithine R and citryl centers N2 R/N5 S; an S,S model fits less well. This supports final product stereochemistry, not a direct free-ion measurement. Source location `PMC2856993 HTML Results, Structure of Staphyloferrin A (sec18), paragraph 2; Figure 2A-C`
SfaB terminal N2-citrylation `RHEA:59141`	produces	adenosine 5'-monophosphate(2-) `CHEBI:456215`	RHEA:59141 Source assertion: The selected Rhea direction assigns CHEBI:456215 to its products with coefficient 1. Source location `rh:59141/rh:products -> http://rdf.rhea-db.org/59140_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59140_compound_2590; rh:compound -> http://rdf.rhea-db.org/Compound_2590; rh:chebi`
SfaB terminal N2-citrylation `RHEA:59141`	produces	diphosphate(3-) `CHEBI:33019`	RHEA:59141 Source assertion: The selected Rhea direction assigns CHEBI:33019 to its products with coefficient 1. Source location `rh:59141/rh:products -> http://rdf.rhea-db.org/59140_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59140_compound_2106; rh:compound -> http://rdf.rhea-db.org/Compound_2106; rh:chebi`
SfaB terminal N2-citrylation `RHEA:59141`	produces	hydron `CHEBI:15378`	RHEA:59141 Source assertion: The selected Rhea direction assigns CHEBI:15378 to its products with coefficient 1. Source location `rh:59141/rh:products -> http://rdf.rhea-db.org/59140_R; rh:contains1 -> http://rdf.rhea-db.org/Participant_59140_compound_3249; rh:compound -> http://rdf.rhea-db.org/Compound_3249; rh:chebi`
L-Ornithine racemization toward D-ornithine `RHEA:11585`	part_of	`MetaCyc:PWY-7990`	MetaCyc:PWY-7990 Source assertion: The complete native pathway explicitly includes ORNITHINE-RACEMASE-RXN; its pathway layout selects the left-to-right biosynthetic direction. Source location `Pathway[@frameid="PWY-7990"]/reaction-list/Reaction[@frameid="ORNITHINE-RACEMASE-RXN"]; reaction-layout[Reaction/@frameid="ORNITHINE-RACEMASE-RXN"]/direction` MetaCyc:ORNITHINE-RACEMASE-RXN Source assertion: The native ornithine racemase reaction is reversible and cross-references RHEA:11587. The pathway selects L- to D-ornithine flux. Source location `Reaction/reaction-direction; dblink[dblink-db="RHEA"]/dblink-oid` RHEA:11585 Source assertion: Rhea master 11584 links bidirectional 11587 and left-to-right 11585, preserving the explicit direction-family bridge. Source location `rh:11584/rh:bidirectionalReaction -> rh:11587; rh:directionalReaction -> rh:11585`
SfaD D-ornithine N5-citrylation `RHEA:59137`	part_of	`MetaCyc:PWY-7990`	MetaCyc:PWY-7990 Source assertion: The complete native pathway explicitly includes RXN-19522; its pathway layout selects the left-to-right biosynthetic direction. Source location `Pathway[@frameid="PWY-7990"]/reaction-list/Reaction[@frameid="RXN-19522"]; reaction-layout[Reaction/@frameid="RXN-19522"]/direction` MetaCyc:RXN-19522 Source assertion: The native equation specifies the ordered citrate ligation with ATP, AMP, diphosphate and proton; its citryl compound identity is less stereospecific than the selected current reaction. Source location `Reaction/left; right; reaction-direction` RHEA:59137 Source assertion: Current master 59136 links the selected left-to-right direction 59137 and defines the complete stereospecific equation independently of native MetaCyc. Source location `rh:59136/rh:directionalReaction -> rh:59137; rh:equation`
SfaB terminal N2-citrylation `RHEA:59141`	part_of	`MetaCyc:PWY-7990`	MetaCyc:PWY-7990 Source assertion: The complete native pathway explicitly includes RXN-19521; its pathway layout selects the left-to-right biosynthetic direction. Source location `Pathway[@frameid="PWY-7990"]/reaction-list/Reaction[@frameid="RXN-19521"]; reaction-layout[Reaction/@frameid="RXN-19521"]/direction` MetaCyc:RXN-19521 Source assertion: The native equation specifies the ordered citrate ligation with ATP, AMP, diphosphate and proton; its citryl compound identity is less stereospecific than the selected current reaction. Source location `Reaction/left; right; reaction-direction` RHEA:59141 Source assertion: Current master 59140 links the selected left-to-right direction 59141 and defines the complete stereospecific equation independently of native MetaCyc. Source location `rh:59140/rh:directionalReaction -> rh:59141; rh:equation`
NWMN_2079 `NCBIProtein:BAF68351.1`	enables Inferred SfaC gene-product role. Neither exact sequence equality nor whole-locus function demonstrates isolated Newman racemase activity or oligomeric state.	L-Ornithine racemization toward D-ornithine `RHEA:11585`	MetaCyc:MONOMER-20490 Source assertion: The native comment explicitly assumes ornithine racemase activity from the functional locus and states that the enzyme was not purified. The mapped UniProt accession is Q2FW73. Source location `Protein[@frameid="MONOMER-20490"]/comment; dblink[dblink-db="UNIPROT"]` NCBIProtein:BAF68351.1 Source assertion: The original Newman entry identifies NWMN_2079 and provides its complete 356-residue sequence; this is genomic protein identity, not a functional assay. Source location `GBSeq[GBSeq_accession-version="BAF68351.1"]/GBSeq_feature-table; GBSeq_sequence` UniProtKB:Q2FW73 Source assertion: The unreviewed NCTC 8325 entry supplies its 356-residue sequence. Comparison with the independently retrieved Newman sequence gives exact equality; functional evidence remains inferred. Source location `/sequence/value; /organism/taxonId; /entryType` PMID:19400778 Source assertion: Table 2 identifies Newman NWMN_2079 as SfaC by amino-acid-racemase similarity. Locus-level product evidence does not establish purified SfaC catalysis. Source location `Results, Table 2 (NWMN_2079); Figure 5; original publisher web text`
NWMN_2082 `NCBIProtein:BAF68354.1`	enables The Newman sequence differs from Q2FW70 at residue 532; exact identity is not claimed. SfaD functional role supported by Newman recombinant biosynthesis plus independently ordered ligation evidence. Exact engineered sequences and native oligomeric sufficiency remain unresolved.	SfaD D-ornithine N5-citrylation `RHEA:59137`	NCBIProtein:BAF68354.1 Source assertion: The versioned entry identifies the Newman coding product, locus and complete protein sequence. Comparison with NCTC 8325 is a separate curation calculation. Source location `GBSeq[GBSeq_accession-version="BAF68354.1"]/GBSeq_feature-table; GBSeq_sequence` PMID:20147287 Source assertion: The study used Newman sfaB and sfaD coding regions for recombinant protein preparations and jointly synthesized staphyloferrin A. This supports the Newman implementation but does not resolve native assemblies. Source location `PMC2856993 HTML Experimental Procedures, Cloning and Protein Expression (sec5), paragraph 2; Staphyloferrin A Synthesis and Purification (sec7)` PMID:19138128 Source assertion: The inspected abstract assigns the first delta-amine citrate ligation to SfnaD and the terminal alpha-amine ligation to SfnaB. Full methods and exact Cotton construct sequences were not inspected. Source location `Europe PMC core resultList.result[0].abstractText` UniProtKB:Q2FW70 Source assertion: The reviewed NCTC 8325 entry assigns this reaction and left-to-right physiological direction with ECO:0000269 citing Cotton. This source annotation is kept separate from Newman protein identity. Source location `/comments/1/reaction; /comments/1/physiologicalReactions; /organism/taxonId` UniProtKB:Q2FW70 Source assertion: The current entry provides the complete NCTC 8325 protein sequence. This supplies the independent comparison source, not an assertion that Newman and NCTC 8325 are the same strain. Source location `/sequence/value; /organism/taxonId`
NWMN_2080 `NCBIProtein:BAF68352.1`	enables The Newman sequence is identical to Q2FW72; strain provenance still remains distinct. SfaB functional role supported by Newman recombinant biosynthesis plus independently ordered ligation evidence. Exact engineered sequences and native oligomeric sufficiency remain unresolved.	SfaB terminal N2-citrylation `RHEA:59141`	NCBIProtein:BAF68352.1 Source assertion: The versioned entry identifies the Newman coding product, locus and complete protein sequence. Comparison with NCTC 8325 is a separate curation calculation. Source location `GBSeq[GBSeq_accession-version="BAF68352.1"]/GBSeq_feature-table; GBSeq_sequence` PMID:20147287 Source assertion: The study used Newman sfaB and sfaD coding regions for recombinant protein preparations and jointly synthesized staphyloferrin A. This supports the Newman implementation but does not resolve native assemblies. Source location `PMC2856993 HTML Experimental Procedures, Cloning and Protein Expression (sec5), paragraph 2; Staphyloferrin A Synthesis and Purification (sec7)` PMID:19138128 Source assertion: The inspected abstract assigns the first delta-amine citrate ligation to SfnaD and the terminal alpha-amine ligation to SfnaB. Full methods and exact Cotton construct sequences were not inspected. Source location `Europe PMC core resultList.result[0].abstractText` UniProtKB:Q2FW72 Source assertion: The reviewed NCTC 8325 entry assigns this reaction and left-to-right physiological direction with ECO:0000269 citing Cotton. This source annotation is kept separate from Newman protein identity. Source location `/comments/1/reaction; /comments/1/physiologicalReactions; /organism/taxonId` UniProtKB:Q2FW72 Source assertion: The current entry provides the complete NCTC 8325 protein sequence. This supplies the independent comparison source, not an assertion that Newman and NCTC 8325 are the same strain. Source location `/sequence/value; /organism/taxonId`
NWMN_2079 `NCBIProtein:BAF68351.1`	has_cofactor Automatic cofactor inference transferred through exact sequence equality; no binding count or direct Newman measurement is asserted.	pyridoxal 5'-phosphate(2-) `CHEBI:597326`	UniProtKB:Q2FW73 Source assertion: The unreviewed NCTC 8325 entry assigns pyridoxal 5-prime-phosphate (CHEBI:597326) through automatic ARBA evidence ECO:0000256; it is not a direct cofactor experiment. Source location `/comments/0/cofactors/0/cofactorCrossReference; /comments/0/cofactors/0/evidences/0; /sequence/value` NCBIProtein:BAF68351.1 Source assertion: The selected entry provides the complete Newman protein sequence. Its identity and genomic origin do not independently establish cofactor binding. Source location `GBSeq[GBSeq_accession-version="BAF68351.1"]/GBSeq_sequence`
NWMN_2080 `NCBIProtein:BAF68352.1`	has_cofactor Qualified native ligase cofactor assignment applied to the Newman role; no independently measured Newman metal specificity, binding stoichiometry or metal-exclusive requirement is claimed.	magnesium(2+) `CHEBI:18420`	MetaCyc:ENZRXN-26283 Source assertion: The native ligase enzymatic-reaction object explicitly lists MG+2 as cofactor and cites Cotton. The cited full article was unavailable; this is a curated database assertion rather than an independently inspected metal assay. Source location `Enzymatic-Reaction[@frameid="ENZRXN-26283"]/cofactor/Compound[@frameid="MG+2"]; cofactor/citation` PMID:20147287 Source assertion: The complete article identifies Newman SfaB and SfaD recombinant preparations used in joint biosynthesis. It supports the selected implementation, not a unique physiological metal or binding stoichiometry. Source location `PMC2856993 HTML sec5 paragraph 2; sec7`
NWMN_2082 `NCBIProtein:BAF68354.1`	has_cofactor Qualified native ligase cofactor assignment applied to the Newman role; no independently measured Newman metal specificity, binding stoichiometry or metal-exclusive requirement is claimed.	magnesium(2+) `CHEBI:18420`	MetaCyc:ENZRXN-26284 Source assertion: The native ligase enzymatic-reaction object explicitly lists MG+2 as cofactor and cites Cotton. The cited full article was unavailable; this is a curated database assertion rather than an independently inspected metal assay. Source location `Enzymatic-Reaction[@frameid="ENZRXN-26284"]/cofactor/Compound[@frameid="MG+2"]; cofactor/citation` PMID:20147287 Source assertion: The complete article identifies Newman SfaB and SfaD recombinant preparations used in joint biosynthesis. It supports the selected implementation, not a unique physiological metal or binding stoichiometry. Source location `PMC2856993 HTML sec5 paragraph 2; sec7`
NWMN_2079 `NCBIProtein:BAF68351.1`	part_of	Staphylococcus aureus subsp. aureus str. Newman `NCBITaxon:426430`	NCBIProtein:BAF68351.1 Source assertion: The source feature explicitly identifies strain Newman and taxon 426430 for this versioned protein. Source location `GBSeq[GBSeq_accession-version="BAF68351.1"]/GBSeq_feature-table/GBFeature[GBFeature_key="source"]/GBFeature_quals`
NWMN_2080 `NCBIProtein:BAF68352.1`	part_of	Staphylococcus aureus subsp. aureus str. Newman `NCBITaxon:426430`	NCBIProtein:BAF68352.1 Source assertion: The source feature explicitly identifies strain Newman and taxon 426430 for this versioned protein. Source location `GBSeq[GBSeq_accession-version="BAF68352.1"]/GBSeq_feature-table/GBFeature[GBFeature_key="source"]/GBFeature_quals`
NWMN_2082 `NCBIProtein:BAF68354.1`	part_of	Staphylococcus aureus subsp. aureus str. Newman `NCBITaxon:426430`	NCBIProtein:BAF68354.1 Source assertion: The source feature explicitly identifies strain Newman and taxon 426430 for this versioned protein. Source location `GBSeq[GBSeq_accession-version="BAF68354.1"]/GBSeq_feature-table/GBFeature[GBFeature_key="source"]/GBFeature_quals`
`MetaCyc:PWY-7990`	part_of	Staphylococcus aureus subsp. aureus str. Newman `NCBITaxon:426430`	PMID:19400778 Source assertion: The Newman locus and product analyses support staphyloferrin A biosynthesis; these organism-level observations do not independently assay every encoded activity. Source location `Results, The NWMN_2082-2079 locus mediates staphyloferrin A biosynthesis; Figure 5; original publisher web text`
L-Ornithine racemization toward D-ornithine `RHEA:11585`	provides_input_for	SfaD D-ornithine N5-citrylation `RHEA:59137`	MetaCyc:PWY-7990 Source assertion: The native ordering puts ORNITHINE-RACEMASE-RXN before RXN-19522; native frames define the shared intermediate without a ChEBI equivalence claim. Source location `Pathway/reaction-ordering[Reaction/@frameid="RXN-19522"]/predecessor-reactions` RHEA:11585 Source assertion: The selected upstream direction produces CHEBI:57668, the same chemical identity independently consumed by the selected downstream direction. Source location `rh:11585/rh:products -> side/rh:contains1 -> participant/rh:compound/rh:chebi` RHEA:59137 Source assertion: The selected downstream direction consumes CHEBI:57668; the explicit common chemical supports material continuity. Source location `rh:59137/rh:substrates -> side/rh:contains1 -> participant/rh:compound/rh:chebi`
SfaD D-ornithine N5-citrylation `RHEA:59137`	provides_input_for	SfaB terminal N2-citrylation `RHEA:59141`	MetaCyc:PWY-7990 Source assertion: The native ordering puts RXN-19522 before RXN-19521; native frames define the shared intermediate without a ChEBI equivalence claim. Source location `Pathway/reaction-ordering[Reaction/@frameid="RXN-19521"]/predecessor-reactions` RHEA:59137 Source assertion: The selected upstream direction produces CHEBI:142972, the same chemical identity independently consumed by the selected downstream direction. Source location `rh:59137/rh:products -> side/rh:contains1 -> participant/rh:compound/rh:chebi` RHEA:59141 Source assertion: The selected downstream direction consumes CHEBI:142972; the explicit common chemical supports material continuity. Source location `rh:59141/rh:substrates -> side/rh:contains1 -> participant/rh:compound/rh:chebi`

References

MetaCyc:PWY-7990 MetaCyc PWY-7990 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:ORNITHINE-RACEMASE-RXN MetaCyc ORNITHINE-RACEMASE-RXN native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:RXN-19522 MetaCyc RXN-19522 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:RXN-19521 MetaCyc RXN-19521 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:MONOMER-20490 MetaCyc MONOMER-20490 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:MONOMER-20491 MetaCyc MONOMER-20491 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:MONOMER-20492 MetaCyc MONOMER-20492 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:ENZRXN-26282 MetaCyc ENZRXN-26282 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:ENZRXN-26283 MetaCyc ENZRXN-26283 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:ENZRXN-26284 MetaCyc ENZRXN-26284 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:L-ORNITHINE MetaCyc L-ORNITHINE native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:CPD-217 MetaCyc CPD-217 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:CPD-21047 MetaCyc CPD-21047 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
MetaCyc:CPD-12589 MetaCyc CPD-12589 native XML object (source version: MetaCyc 22.5; retrieved 2026-10-11; complete native XML response)
KEGG:M00876 KEGG M00876: Staphyloferrin A biosynthesis, L-ornithine => staphyloferrin A (source version: Original response retrieved 2026-10-11; hash covers complete response body)
NCBIProtein:BAF68351.1 NCBI GenPept BAF68351.1 Newman protein identity (source version: GenPept original three-entry batch retrieved 2026-10-11; hash covers entire XML batch)
NCBIProtein:BAF68352.1 NCBI GenPept BAF68352.1 Newman protein identity (source version: GenPept original three-entry batch retrieved 2026-10-11; hash covers entire XML batch)
NCBIProtein:BAF68354.1 NCBI GenPept BAF68354.1 Newman protein identity (source version: GenPept original three-entry batch retrieved 2026-10-11; hash covers entire XML batch)
UniProtKB:Q2FW73 UniProtKB Q2FW73 original entry; NCTC 8325 scope (source version: UniProt release 2026_03; original JSON retrieved 2026-10-11)
UniProtKB:Q2FW72 UniProtKB Q2FW72 original entry; NCTC 8325 scope (source version: UniProt release 2026_03; original JSON retrieved 2026-10-11)
UniProtKB:Q2FW70 UniProtKB Q2FW70 original entry; NCTC 8325 scope (source version: UniProt release 2026_03; original JSON retrieved 2026-10-11)
PMID:19138128 Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. (source version: Cotton et al. 2009; indexed abstract only; hash covers original Europe PMC core JSON, not full article)
PMID:20147287 The Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding Pocket (source version: Grigg et al. 2010; complete original PMC HTML inspected; Figure 2A image separately inspected)
PMID:19400778 Characterization of staphyloferrin A biosynthetic and transport mutants in Staphylococcus aureus. (source version: Beasley et al. 2009; full original publisher text inspected through web access on 2026-10-11; no local full-body hash; indexed abstract separately retained)
RHEA:11585 Rhea 11585 exact directional reaction and side graph (source version: Rhea 142, 2026-09-02; digest covers complete original gzip RDF)
RHEA:59137 Rhea 59137 exact directional reaction and side graph (source version: Rhea 142, 2026-09-02; digest covers complete original gzip RDF)
RHEA:59141 Rhea 59141 exact directional reaction and side graph (source version: Rhea 142, 2026-09-02; digest covers complete original gzip RDF)
CHEBI:142973 ChEBI 255 chemical structures, charges and stereochemical names (source version: ChEBI 255 Semantic SQL; digest covers full uncompressed original database)

Curation history

2026-10-11T14:02:37Z codex
- CREATE — Prepare complete staphyloferrin A biosynthesis from original evidence
  Copy the full three-transformation PWY-7990 route with versioned Newman protein identities, explicit inferred SfaC and cofactor roles, native versus current stereochemical distinctions, and construct/source-access limitations. Original author inputs and independent preflight are preserved. Shared authority integration, full corpus gates, canonical scientific review and publication remain pending.
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